# dir.com.scop.txt 
# SCOP release 1.69 (July 2005)  [File format version 1.00]
# http://scop.mrc-lmb.cam.ac.uk/scop/
# Copyright (c) 1994-2005 the scop authors; see http://scop.mrc-lmb.cam.ac.uk/scop/lic/copy.html
46457 ! core: 6 helices; folded leaf, partly opened
46459 ! lack the first helix (A)
46462 ! Globin li637
105305 !SQ P73925
105306 !SQ P73925
105097 !SQ Q10784
105284 !SQ Q10784
105261 !SQ Q10784
74660 ! lack the first helix but otherwise is more similar to conventional globins than the truncated ones
108201 !SQ O76242
46463 ! Heme-binding protein
71726 ! component III
71725 ! component IV
71643 ! component IV
71642 ! component III
15027 ! apo form complexed with biliverdin IX
15031 ! apo form complexed with biliverdin IX
85238 ! combined rietveld and stereochemical restraint refinement
15035 ! reconstituted with cobalt
15037 ! reconstituted with cobalt
15040 ! reconstituted with cobalt
15099 ! neutron structure of fully deuterated protein
103835 !SQ P02185
107815 !SQ P02185
107818 !SQ P02185
15262 ! recombinant hemoglobin rhb1.1
81065 ! genetically crosslinked hemoglobin
81049 ! genetically crosslinked hemoglobin
81073 ! genetically crosslinked hemoglobin
15277 ! recombinant hemoglobin rhb1.0
15279 ! recombinant hemoglobin rhb1.2
15289 ! recombinant hemoglobin; two alpha subunits fused in a single chain
81061 ! genetically crosslinked hemoglobin
81057 ! genetically crosslinked hemoglobin
79248 ! A fourth quaternary structure
15350 ! recombinant hemoglobin; two alpha subunits fused in a single chain
109416 !SQ P83134
108365 !SQ Q8AYM0
108361 !SQ Q8AYM0
108357 !SQ Q8AYM0
15439 ! recombinant hemoglobin rhb1.1
15456 ! recombinant hemoglobin rhb1.0
15458 ! recombinant hemoglobin rhb1.2
15466 ! homo(beta)tetramer
15492 ! homo(beta)tetramer
79249 ! A fourth quaternary structure
61588 ! hemoglobin Bart's (gamma4)
61590 ! hemoglobin Bart's (gamma4)
109417 !SQ P83133 
108366 !SQ Q8AYM1
108362 !SQ Q8AYM1
108358 !SQ Q8AYM1
104476 !SQ Q9ER97
108013 !SQ Q8WWM9 18-171
108090 !SQ Q8WWM9 18-171
107960 !SQ Q8WWM9 18-171
108375 !SQ Q8WWM9 18-171
107320 !SQ Q9HX49
46532 ! oligomers of two different types of globin-like subunits containing two extra helices at the N-terminus ! binds a bilin chromophore
46548 ! contains two Fe4-S4 clusters
46554 ! includes the N-terminal tail and the linker to domain 2
46556 ! 2 helices; antiparallel hairpin, left-handed twist
46559 ! C-terminal domain is FKBP-like
105341 !SQ P10971
104827 !SQ P38514 # ! Structural genomics target
91617 ! includes unstructured clathrin substrate binding region; residues 1-70
100983 ! structural genomics
65191 ! extended at the C-terminus
46575 ! fold is similar to the chaperone J-domain ?
46580 ! contains one or two beta-hairpins at the tip of alpha-hairpin
46586 ! protein kinase effector domain
15705 ! first HR1 domain complexed with RhoA
99827 ! second HR1 domain
46589 ! formerly a class II aminoacyl-tRNA synthetase N-domain
83811 ! preliminary structure of ligand-free enzyme; CA-atoms only
81671 ! inserted in the C-terminal NAT-like domain
81672 ! proposed to bind tRNA-Gly
105078 !SQ P11387 203-767
46606 ! delta subunit in mitochondria ! this domain unfolds when bound to the gamma subunit
15775 ! iron-substituted
46622 ! active with either Fe or Mn
107796 !SQ P19665
107804 !SQ P19665
109631 ! similar structure to L29p (scop_sf 46561); contains extra short helix; forms homodimer: an open bundle  
108000 !SQ Q57471
107993 !SQ Q57471
107045 !SQ P18274 7-151 
63445 ! tandem repeat of two calcium-binding loop-helix motifs, distinct from the EF-hand
93044 ! complexed with cohesin domain
63450 ! helix-extended loop-helix; parallel helices
60825 ! LEM-like domain; res. 2-57
60826 ! LEM domain; res. 103-159
83292 ! the two domain structures are superimposed on each other
109639 ! 2 helices: one short, one long; aromatic-rich iterface
108393 !SQ Q8BG62 4-54 # ! Structural genomics target
46625 ! core: 3 helices; folded leaf, opened
46626 ! covalently-bound heme completes the core
15813 ! Cytochrome c557: improperly folded c552
104662 !SQ P04164
104755 !SQ P04164
107707 !SQ P00044
74519 ! zinc-substituted
15870 ! imidazole complex
15872 ! imidazole complex
107709 !SQ P00004
103838 !SQ P99999
108901 !SQ P00094
68950 ! close homologue of SHP
46669 ! the other subunit is a flavoprotein
107958 !SQ P14774 49-197
46672 ! the C-terminal domain is a 8-bladed beta-propeller
46673 ! formerly <i>Thiosphaera pantotropha</i>
104273 !SQ P00125
104243 !SQ P00125
105896 !SQ P00125
15956 ! disordered domain
46680 ! duplication: consists of two cytochrome c type domains
81677 ! two-domain cytochrome c with novel domain arrangement
81678 ! cysteine persulfide(cys sulfane) heme coordination
46685 ! duplication: contains two cytochrome c-type domains
105136 !SQ P83787
105134 !SQ P83787
68957 ! duplication: tandem repeat of two cytochrome c-like domains
46688 ! core: 3-helices; bundle, closed or partly opened, right-handed twist; up-and down
46689 ! consists only of helices
79112 ! chimera with maltose-binding protein
79114 ! chimera with maltose-binding protein
46697 ! atypical Homeodomain with a large insertion into HTH motif
62951 ! complexed to AT-rich DNA
81681 ! single domain composed of a homeodomain-homology N-terminal region (1245-1295) and the prospero-specific C-terminal region (1296-1396) that forms a 4-helical bundle
107853 !SQ Q8R1H0
107713 !SQ P34257 2-104
46735 ! contains additional helix at each terminus
46740 ! duplication
83338 ! repeat 2
83337 ! repeat 2
83332 ! repeat 1
83336 ! repeats 2 & 3
16036 ! repeat 2
16032 ! repeat 3
16031 ! repeat 3
16035 ! repeat 3
16038 ! repeat 1
16033 ! repeat 2
16034 ! repeat 3
16040 ! repeats 2 & 3
16037 ! repeat 1
16042 ! repeats 2 & 3
65728 ! repeat 1 is partly disordered
16044 ! repeats 2 & 3
65732 ! repeats 2 & 3
107823 !SQ Q80TB4 1951-2032 # ! Structural genomics target
100998 ! myb-related probable DNA-binding motif
92827 ! includes alpha-helical spacer, residues 851-891, separating SANT and SLIDE domains
81683 ! plant myb-related DNA-binding motif
46748 ! duplication: consists of two domains of this fold
46753 ! duplication: consist of two domains of this fold
46756 ! duplication: tandem repeat of two similar domains
16052 ! the N-terminal domain only
71440 ! low resolution solution structure
48285 ! includes N-terminal dimerisation subdomain
48287 ! includes N-terminal dimerisation subdomain
46759 ! duplication: consists of two structural repeats bipartite HTH protein
16054 ! CASP3
16066 ! class d variant
16067 ! class d variant
16071 ! class d; complex with 4-epi-tetracycline
104973 !SQ P23217
104616 !SQ P23217
104608 !SQ P23217
105042 !SQ P23217
100722 ! structural genomics
97625 ! structural genomics
106428 !SQ P96222
109653 ! gamma-butyrolactone receptor
107858 !SQ O66122
107862 !SQ O66122
106297 !SQ Q8ZQN9 # ! Structural genomics target
105539 !SQ P42105
109659 ! contains extra N-terminal dimerisation subdomain: alpha-hairpin (27-72) dimer is a four-helical bundle with right-handed twist
105075 !SQ P23848 27-120
106333 !SQ P16455 6-176
106337 !SQ P16455 6-176
46774 ! contains extra helices at both N- and C-termini
105127 !SQ O14497 617-736
46785 ! contains a small beta-sheet (wing)
46787 ! the middle domain is an alpha+beta fold somewhat similar to the SH2 fold ! C-terminal domain has SH3-like common fold
71592 ! structural genomics
101008 ! AT-rich DNA-binding protein p25
101009 ! CASP5
109564 !SQ Q9X2V5
46797 ! N-terminal domain has double beta-helix fold
68967 ! Swapped dimer with the "wing" C-terminal strands
101010 ! archaeal feast/famine regulatory protein
101011 ! identical sequence to Pyrococcus sp. ot3 protein
46801 ! The N- and C-terminal helical extensions to the common fold form the dimer interface
104770 !SQ P30340
104780 !SQ P30340
104778 !SQ P30340
104774 !SQ O85142
104776 !SQ O85142
63379 ! The N- and C-terminal helical extensions to the common fold form the dimer interface
61239 ! Fusion protein with E. coli MBP
88977 ! duplication: tandem repeat of two SarR-like domains assembled together as in the SarR dimer
48292 ! closely related to SarR but adopts a different fold; possible experimental artifact?
98438 ! structural genomics
99159 ! structural genomics
81690 ! homologous to the MarR-like family in the DNA-binding region but dimerizes differently through the N- and C-terminal helical extensions to the common fold
101016 ! homologous to the MarR-like family in the DNA-binding region but has a different dimerisation subdomain
98788 ! complexed with DNA
94187 ! DNA-binding domain only
105429 !SQ Q9K4N1
16113 ! CASP4
60849 ! complex with fadB operator
46808 ! contains long helix in the C-terminal extension; forms dimer similar to the LysR-like dimer
16117 ! CASP1
59647 ! complexed with DNA
88979 ! contains long helix in the C-terminal extension; forms dimer similar to the RTP dimer
46810 ! contains beta-hairpin in the N-terminal extension and two helices in the C-terminal extension
81156 ! molybdate-activated form
46813 ! The N- and C-terminal helical extensions to the common fold form the dimer interface (distinct from that of ArsR-like family)
101024 ! contains extra N-terminal helix
101027 ! contains extra N-terminal helix and an alpha+beta dimerisation subdomain
46816 ! duplication: tandem repeat of two "winged helix" domains arranged with the pseudo twofold symmetry
83556 ! inactive, dimeric N-terminal domain
46819 ! follows the extended AAA-ATPase domain 
46822 ! contains the N- and C-terminal helical extensions to the common fold
101030 ! follows the tandem AAA-ATPase domain
74684 ! duplication: tandem repeat of four "winged helix" domains
46825 ! duplication: consists of three elaborated "winged helix" domains
63475 ! unknown function
101035 ! evolved a different function; binds SAM and SAH
107375 !SQ Q06528
107371 !SQ Q06528
101037 ! duplication: contains two similar globular domains
99884 ! N-terminal globular domain, GI
99883 ! C-terminal globular domain, GII
99398 ! N-terminal globular domain, GI
63481 ! peptide-recognition motif
77066 ! complexed with Fcp1 C-terminal peptide, chain B
87171 ! complexed with Fcp1 C-terminal peptide, chain B
46845 ! peptide-recognition motif
16150 ! complexed with the fragment 73-88 of uracil DNA glycosylase UNG2
63483 ! membrane-binding domain
46847 ! heterodimer of two homologous chains
46853 ! Pfam 02295
105504 !SQ Q9DHS8 1-75
46856 ! C-terminus passes through the first loop
104085 !SQ P33120
101051 ! Pfam 05383; RNA-binding domain
46887 ! circularly permuted version of the "winged helix" fold
107816 !SQ O88544 296-366 # ! Structural genomics target
109674 ! contains long helix in the C-terminal extension; forms dimer similar to the RTP and LysR dimers 
106749 !SQ P20222
109677 ! contains long helix in the C-terminal extension; forms dimer similar to the RTP and LysR dimers 
104836 !SQ Q5W1E8
109680 ! The N- and C-terminal helical extensions to the common fold form the dimer interface, distinct from other known families
105506 !SQ O28271 # ! Structural genomics target
109683 ! similar domain organization to the transcriptional regulator IclR
106013 !SQ Q9WZV5 # ! Structural genomics target
109403 !SQ Q8R4E9 179-365
109689 ! C-terminal part of Pfam 06272
105131 !SQ Q9UBQ5
109692 ! duplication: tandem repeat of two "winged-helix" domains 
107685 !SQ Q12483 
107687 !SQ Q06696 396-564
107691 !SQ P47142
109566 !SQ P71036 4-130
107226 !SQ O30245 # AF2426
107236 !SQ O30245 # AF2426
107240 !SQ O30245 # AF2426
46894 ! binds to DNA and RNA polymerase; the N-terminal, receiver domain belongs to the CheY family
46895 ! contains 4-stranded meander beta-sheet in the N-terminal extension
46900 ! contains additional, fourth helix in the C-terminal extension
63488 ! single-domain protein homologous to the C-terminal domain of NarL
77111 ! C-domain only
87783 ! DNA-binding domain only
46903 ! elaborated with additional helices
16239 ! CASP4
48295 ! contains an extra shared helix after the HTH motif
48296 ! intertwined dimer of identical 6-helical subunits
91278 ! domain swapped structure
81695 ! monomeric; contains additional N-terminal helices
83981 ! domain IV only; complexed with DnaA box DNA
16241 ! complex with a fragment of 23S rRNA
105328 !SQ P14122 67-136
16250 ! partly disordered
46917 ! links two duplicated two-domain units formed by domains 1-2 and 4-5
46920 ! Zn-binding site is near the C-terminus
46925 ! Zn-binding site is near the N-terminus
105791 !SQ Q9WX78 
105792 !SQ Q9WX78 
73000 ! sigma4 domain only
73002 ! sigma4 domain only
73405 ! sigma4 domain only
109706 ! structural and detectable sequence similarity to Sigma4 domain; contains extra C-terminal all-alpha oligomerization subdomain; forms different, helix-swapped dimers
105356 !SQ P67253 # ! Structural genomics target
109709 ! contains HTH motif in the common core; also contains extra N-terminal helix and C-terminal subdomain of 4 helices (left-handed superhelix) 
109710 ! [N-terminal half of Pfam 06613]
104826 !SQ P07674 137-252 # structure of the C-terminal domain (297-358) is determined separately; scop_sp 69244
108943 !SQ Q9LCY0 # Fragment
81602 ! topologically similar to the DNA/RNA-binding bundles; distinct packing
81701 ! Flj21157
100222 ! CASP5; supersedes original entry 1H40
101061 ! Gene 0.3 protein; active form is a dimer
104479 !SQ P35659 309-375
46928 ! 3 helices; bundle, right-handed twist
46929 ! possibly related to UBA-like domains
46931 ! tetramer; binds Holliday junction
16288 ! C-terminal UBA domain
16289 ! C-terminal UBA domain
93440 ! flexible linkers excluded
71207 ! internal UBA domain
101063 ! ubiquitin-binding protein p62
107295 !SQ P21734
108528 !SQ P57080 1-67 # ! Structural genomics target
81255 ! complexed with FxFG nucleoporin peptide
85024 ! part of the C-terminal helix-swapped homodimer
87749 ! partly disordered, helix-swapped homodimer
89003 ! gene product DmpG
105963 !SQ P96420
109725 ! duplication: contains two domains of this fold, connected with a helical linker
109727 ! d1: 307-367; d2: 416-459
105057 !SQ Q70AC7 3-474
105066 !SQ Q70AC7 3-474
105073 !SQ Q70AC7 3-474
105061 !SQ Q70AC7 3-474
105235 !SQ Q70AC7 3-474
107682 !SQ Q70AC7 3-474
101071 ! Sec14-like protein 2; contains extra C-terminal beta-sandwich domain 
104014 !SQ O76054
16298 ! structural genomics
106705 !SQ O29759
104093 !SQ O29759 # ! Structural genomics target
109732 ! possibly related to UBA-like domains 
107821 !SQ Q69ZS7 51-120 # ! Structural genomics target
106381 !SQ P74881
81297 ! core: 3-4 helices
46946 ! contains a helix-two turns-helix (H2TH) motif
46947 ! contains 3 helices and a beta-hairpin in the core and a non-globular C-terminal extension
81626 ! contains 4 helices in the core
96892 ! bound to 5,6-Dihydrouracil (DhU) containing DNA
75911 ! covalent-DNA intermediate
75908 ! bound to abasic-site containing DNA
75920 ! DNA estranged guanine mismatch recognition complex
75917 ! DNA estranged thymine mismatch recognition complex
96889 ! bound to 8-Oxoguanine (OxoG) containing DNA
75914 ! DNA end-product structure
75875 ! covalently trapped with DNA
106787 !SQ P42371
104164 !SQ P42371
104161 !SQ P42371
104190 !SQ P42371
104518 !SQ P50465
104521 !SQ P50465
104515 !SQ P50465
106772 !SQ Q96FI4 1-333
46954 ! core: 3 helices; architecture is similar to that of the "winged helix" fold but topology is different
46956 ! duplication: contains two such domains related by pseudo dyad
105414 !SQ P12755 91-192
46962 ! includes a dimerisation, antiparallel coiled-coil subdomain
46963 ! followed by long alpha-helical linker
104843 !SQ P39075
104842 !SQ P71039 1-109
101073 ! copper efflux regulator
101075 ! Zn(II)-responsive regulator of ZntA
95498 ! zinc-binding, dimerisation subdomain only
95501 ! zinc-binding, dimerisation subdomain only
95499 ! zinc-binding, dimerisation subdomain only
46891 ! kinked C-terminal helix
104936 !SQ P03699 1-55
84734 ! C-terminally truncated variant
46965 ! 3 helices; bundle, closed, left-handed twist; up-and-down
16312 ! the crystal structure is an intertwined dimer
16318 ! repeats 16 and 17
16319 ! monomeric NMR structure
93640 ! N-terminal repeat; includes extra N-terminal helix; tetramerisation region
16321 ! two central spectrin-like repeats
60957 ! the rod domain: homodimer of four-repeat fragments
46974 ! form trimers with 9 helices in a bundle
16333 ! bound to xiap-bir3 domain
63492 ! Pfam 02179
101080 ! Bcl2-associated athanogene 3
107830 !SQ Q8CI32 1-86 # ! Structural genomics target
84017 ! structure of a two-helical fragment bound to ARF1
100929 ! this domain is associated with the N-terminal ENTH-like domain
90358 ! complex with inositol(4,5)p2
46989 ! the C-terminal helix is shorter that the other two helices
105086 !SQ P26649 # ! Structural genomics target
109751 ! the bundle twist angle is close to zero (small positive value); similar to the RRF alpha-helical bundle, scop_sf 55194    
108983 !SQ Q9NZD4 3-94
108984 !SQ Q9NZD4 3-94
108985 !SQ Q9NZD4 3-94
109755 ! duplication: consists of two sequence each repeats adopting this fold 
106025 !SQ Q9X256 # ! Structural genomics target
46996 ! 3 helices; bundle, closed, left-handed twist; up-and-down; mirror topology to the spectrin-like fold
16344 ! domain D
16345 ! domain B, incomplete
16346 ! domain E
16347 ! domain E
16349 ! domain E
16348 ! domain E
16350 ! domain B
16351 ! domain B
84665 ! chain B is domain Z; chain A is a domain Z-based artificial affibody, Zspa-1
95631 ! domain Z
16352 ! domain Z
98977 ! domain B
83441 ! chain A is domain Z; chain B is a domain Z-based artificial affibody, Zspa-1
106825 !SQ Q51911 213-265
81711 ! dimeric
89013 ! family 57 glycoside hydrolase; overall domain organization is similar to that of the alpha-mannosidase family
88693 ! family 38 glycoside hydrolase; overall domain organization is similar to that of the 4-alpha-glucanotransferase family
89016 ! the single-chain precursor is processed into 5 peptides; heavily glycosylated
99329 ! structural genomics
106578 !SQ Q89728 459-507 ! complexed with peptide from the measles virus N protein (SQ Q995N1 58-77)
101094 ! duplication: consists of two domains of this fold
90345 ! complexed with peptide, chain B
90339 ! complexed with peptide, chain B
99201 ! C-terminal subdomain only; forms helix-swapped dimer
47004 ! 3 helices; bundle, closed, right-handed twist; up-and-down
109151 !SQ P11961 118-170
47013 ! 3 helices; bundle, closed, left-handed twist, up-and-down
47026 ! core: 3 helices; bundle, closed, left-handed twist; up-and-down
103872 !SQ P07107
105529 !SQ P26038 4-297
83958 ! complexed with the icam-2 cytoplasmic peptide, chain B
68980 ! the neurofibromatosis 2 tumor suppressor protein
79172 ! chimera with an integrin beta3 peptide, chain A
79221 ! chimera with an integrin beta3 peptide, chains A and C
79229 ! chimera with an integrin beta3 peptide, chains A, C, E and G
47039 ! 3 helices; bundle, partly opened
98789 ! complexed with the transactivation peptide of c-myb, chain B
47044 ! 3 helices, the first one is shorter than the other two; bundle, partly opened
47049 ! 3 short helices; irregular array
107965 !SQ P09327 792-826
107966 !SQ O75366 784-819
47054 ! 3 short helices; irregular array
47059 ! 3 helices; irregular array
47064 ! contains additional N-terminal helix that forms a separate unit
16385 ! complex with an rRNA fragment
16386 ! complex with an rRNA fragment
84470 ! complex with an rRNA fragment
47071 ! 3 helices; irregular array; disulfide-rich
63500 ! Core: 3 helices; irregular array; disulfide-rich
62516 ! CASP4
47076 ! 3 helices; irregular array
47081 ! core: 3 helices; bundle, closed, right-handed twist; up-and-down
16415 ! CASP4
47089 ! core: 3 helices; bundle, closed, left-handed twist; parallel
47092 ! probable peptidoglycan-binding domain
47094 ! 3 helices; irregular array
47097 ! duplication: contains HMG-box domains
16417 ! domain A
16420 ! domain A
16418 ! domain B
16419 ! domain B
16421 ! domain B
16422 ! domain B
16423 ! domain B
16424 ! domain B
103840 !SQ P17741 1-77 
103833 !SQ P17741 89-163
103832 !SQ P17741 88-163
68982 ! Contains 6 HMG-box domains
68341 ! HMG box 1
73708 ! HMG box 5
73709 ! HMG box 5
108392 !SQ P25976 388-383 # ! Structural genomics target
108391 !SQ P25976 567-655 # ! Structural genomics target
47112 ! core: 3 helices; long middle helix is flanked at each end with shorter ones
47114 ! form octamers composed of two copies of each of the four histones
107534 !SQ P02263
107535 !SQ P02279
107536 !SQ P84229
107537 !SQ P62801
47135 ! TAFii42 and TAFii62 form heterotetramer similar to (H3-H4)2
47137 ! TAFii42 and TAFii62 form heterotetramer similar to (H3-H4)2
81720 ! lacks the third helix, forms a heterodimer with TAF(II)-20 similar to H2A-H2B
81722 ! forms a heterodimer with TAF(II)-135 similar to H2A-H2B
81724 ! forms a heterodimer with Nf-Yc2 similar to H2A/H2B
81726 ! forms a heterodimer with Nf-Yb3 similar to H2A/H2B
47143 ! core: 3 helices; bundle, open
47148 ! contains irregular N-terminal subdomain
47152 ! duplication: consists of two domains of this fold
81729 ! core: 3 helices; irregular array
81732 ! consists of a globular N-domain and extended C-terminal tail
47161 ! core: 4 helices; bundle, closed or partly opened, left-handed twist; up-and-down
47163 ! Can exist in a coiled-coil oligomeric form, see PDB entry 1AV1 ! family may also include the five-helical bundle protein Apolipophorin-III
16521 ! truncation mutant 165
16522 ! truncation mutant 165
16525 ! truncation mutant 165
47175 ! Heme-containing proteins
78705 ! b562ril, a redesigned four helix bundle
16543 ! apo-form
47189 ! Iron-binding proteins
47218 ! The structure of the proteasome complex with this protein from (<i>Trypanosoma brucei</i>) is available </i>(<a href="../pdb.cgi?pdb=1fnt">1fnt</a>)<i>; however, PDB entry 1FNT designates protein chains by both upper case and lower case letters creating problems with its processing and presentation; the proteasome activator pa26 chains are designated by lower case letters (c;d;e;f;g;h;i;j;k;l;m;n;o;p)
47221 ! possible duplication: contains several domains of this fold ! The listed PDB entries contain different large fragments but not the whole proteins
16627 ! N-terminal, dimerization and beta-catenin binding domain
16626 ! chimera of the N-terminal domain of alpha-catenin and beta-catenin fragment (chain B)
60672 ! middle domain; contains two domains of this fold
73652 ! CASP4
16629 ! tail domain
106189 !SQ P12003 1-253  ! complexed with Talin 1 fragment (SQ P26039 605-628), chain B
106007 !SQ P12003 ! full-length protein containing eight four-helix bundle domains
97609 ! head domain; contains two domains of this fold; complexed with separate tail domain of the same or closely related protein
97610 ! tail domain; complexed with separate head domain of the same or closely related protein
106125 !SQ P18206 1-257 ! head domain; contains two domains of this fold; complexed with talin fragment, chain B (SQ Q9Y490 607-631)
97607 ! head domain; contains two domains of this fold; complexed with talin fragment, chain B
67904 ! swapped dimer
93633 ! complexed with paxillin ld4 motif, chains D and F
93636 ! complexed with paxillin ld4 motif, chains D, E and F
93639 ! complexed with paxillin ld2 motif, chains D and F
104321 !SQ Q00944 RE 920-1053
101114 ! PsbQ protein of photosystem II
47226 ! contains additional, fifth helix at the N-terminus
107224 !SQ Q56310 4-104
47233 ! contains extra helices in the loops at one end of the bundle
101116 ! can form closed, open and helix-swapped bundles 
93466 ! complexed with a flagelin fragment, chain B 
100645 ! structural genomics; swapped dimer
108889 !SQ Q9WZ40 # ! Structural genomics target
89018 ! a mammalian FAD-dependent sulfhydryl oxidase
81741 ! function unknown; form complex with putative catalytic subunit HI0073 (see 1no5)
77145 ! structural genomics
89023 ! Family 5 probable bi-partite nucleotidyltransferase subunit; predicted partner is putative catalytic subunit TM0614
86615 ! structural genomics
99334 ! structural genomics; dimeric structure is more similar to that of HI0074 (1jog) than more closely related TM0613 (1ou3)
81592 ! N-terminal catalytic domain is followed by an all-alpha domain
75880 ! CA-atoms only, mutant protein sequence
108350 !SQ P30870 1-437 
101127 ! tRNA-mimic
104439 !SQ P80734
104463 !SQ P80734
104427 !SQ P80734
104415 !SQ P80734
104454 !SQ P80734
106595 !SQ P80735
106581 !SQ P80735
106573 !SQ P80735
109775 ! contains extra alpha+beta subdomain formed by the N- and C-termini. 
106159 !SQ Q9DBG5 206-431
107824 !SQ Q8C4Q6 1-115 # ! Structural genomics target
63519 ! core: 4 helices; bundle, closed, right-handed twist; 1 crossover connection
63520 ! duplication: consists of two domains of this fold
47239 ! core: 4 helices; bundle, closed, left-handed twist; 1 crossover connection
47240 ! contains bimetal-ion centre in the middle of the bundle
105230 !SQ P24931
105232 !SQ P24931
92008 ! structural genomics
90807 ! segment-swapped dimer
100837 ! structural genomics
47244 ! binds heme between two subunits; 24-mer
108823 !SQ Q9X0L2 # ! Structural genomics target
47251 ! ferritin homolog that binds to and protects DNA
108537 !SQ Q8VP75
108531 !SQ Q8VP75
108549 !SQ Q8VP75
104675 !SQ Q8N4E7
109217 !SQ P11157 
109216 !SQ P11157 
63142 ! heterodimer with Y4 isoform
105769 !SQ P09938
63143 ! heterodimer with Y2 isoform
105771 !SQ P49723
106126 !SQ O84835
108180 !SQ Q50549 10-291
93522 ! structural genomics
109788 ! contains the TouB(TmoB)-binding YHS (sub)domain (Pfam 04945) in the C-terminal part (401-450)
106220 !SQ O87798
106226 !SQ O87798
106223 !SQ O87798
106221 !SQ O87802
106227 !SQ O87802
106224 !SQ O87802
89028 ! crossover loop goes across a different side of the 4-helical bundle; no internal metal-binding site
97830 ! structural genomics; NESG target SR128
85923 ! structural genomics
85740 ! structural genomics
47265 ! core: 4 helices; bundle, closed; left-handed twist; 2 crossover connections
47266 ! there are two different topoisomers of this fold with different entanglements of the two crossover connections
16830 ! mouse-human chimera, residues 48-81 are from human sequence
77356 ! phage display derived variant
47287 ! long chain cytokine with a short-chain cytokine topology
101140 ! long chain cytokine with a short-chain cytokine topology
47293 ! intertwined dimer
47295 ! forms dimer similar to the Flt3 ligand and SCF dimers
16868 ! CA-atoms only
47297 ! forms dimer similar to the M-CSF and SCF dimers
47299 ! forms dimer similar to the M-CSF and Flt3 ligand dimers
95201 ! complexed with a small molecule inhibitor
95322 ! complexed with a small molecule inhibitor
16884 ! mutant with truncation at both N- and C-termini and 14 residue changes
47305 ! contains an additional helix in one of the crossover connections
47306 ! intertwined dimer, similar to interferon-gamma
62704 ! complexed with IL-10 receptor 1 (IL-10R1)
16891 ! CA-atoms only
16892 ! CA-atoms only
16898 ! CA-atoms only
47318 ! intertwined dimer
16910 ! a single-chain variant
16920 ! CA-atoms only
16914 ! biologically active single chain mutant
16921 ! CA-atoms only
47322 ! core: 4 helices; bundle; one loop crosses over one side of the bundle
47325 ! this domain follows the Rossmann-fold catalytic domain of class I aaRS
105063 !SQ Q9V011 1-606 # C-domain 616-722 is solved separately: 1MKH
47330 ! contains additional alpha+beta and Zn-binding domains in the C-terminal extension
47331 ! includes additional alpha+beta (sub)domain at the C-terminus
83812 ! preliminary structure of ligand-free enzyme; CA-atoms only
76641 ! The C-terminal region (residues 815-878) is invisible in the electron density
86764 ! The C-terminal region (residues 815-878) is invisible in the electron density
86773 ! The C-terminal region (residues 815-878) is invisible in the electron density
47335 ! 4 helices, bundle; helix 3 is shorter than others; up-and-down
106666 !SQ P02901
59688 ! complexed with holoACP synthase
108690 !SQ Q9WY19 # ! Structural genomics target
99475 ! computationally designed interface with the colicin E7 DNase domain
16954 ! extended at the C-terminus to include a 14-residue GAG p2 domain
16959 ! C-terminal domain only
47363 ! 4 helices; bundle; minor mirror variant of up-and-down topology
16969 ! complexed with acetylated H4 peptide
71746 ! complexed with HIV-1 tat peptide, chain A
71843 ! complexed with p53 peptide, chain A
47203 ! multidomain flavoprotein; N-terminal domain is all-alpha; the middle domain is open (5,8) barrel
106717 !SQ P11310 34-421
101146 ! involved in biosynthesis of methoxymalonyl extender unit of fk520 polyketide immunosuppressant
105585 !SQ Q92947
105587 !SQ Q92947
74714 ! duplication: tandem repeat of this fold
101148 ! contains a short alpha-hairpin at the N-terminal extension
101149 ! Pfam 04043
101152 ! common fold is elaborated with additional short helices; contains a zinc-binding site
104786 !SQ Q7T1M9 33-215
106781 !SQ P38582
47379 ! 4 helices; dimer of identical alpha-hairpin subunits; bundle, closed, left-handed twist
16977 ! single-residue mutant with a changed dimer topology
16979 ! a multiple mutant with a repacked hydrophobic core and a new dimerization mode
76235 ! single-residue mutant with a changed dimer topology
16988 ! a multiple mutant with a repacked hydrophobic core and a new dimerization mode
104642 !SQ P03051 ! 5-residue deletion mutant; tetramer
105693 !SQ P20215
47390 ! 4 helices; bundle, closed, right-handed twist
47391 ! dimer of identical alpha-hairpin motifs
89042 ! 4 helices; bundle, closed, right-handed twist
89043 ! dimer of identical alpha-hairpin motifs
47395 ! 4 helices; bundle, closed, right-handed twist
47396 ! dimer of non-identical alpha-hairpins
47397 ! heterodimer of two homologous chains
47400 ! 4 helices; bundle, closed, left-handed twist
47401 ! disulfide-linked heterodimer of similar alpha-hairpin subunits
47405 ! 4 helices; bundle, closed, right-handed twist
47406 ! intertwined heterodimer of two homologous chains
17001 ! CASP3; complexed with SinI anti-repressor
17002 ! CASP3; complexed with SinR repressor dimerisation domain
95467 ! fused interacting segments 
109805 ! interlocking dimer with longer helices and aromatic-rich core
104500 !SQ O14492 21-85
47412 ! core: 4 helices; folded leaf, closed
47415 ! canonical 4-helical fold
81748 ! atypical POU domain with extra N-terminal helix
47419 ! consists of different sequence families of HTH repressors of phage origins
17027 ! CA-atoms only
47423 ! contains a short additional helix at C-terminus
105888 !SQ P16117 10-62 ! design mutant devoid of hydroxyl groups
47425 ! contains a short additional helix at C-terminus
47427 ! contains a short additional helix at C-terminus
47428 ! the fourth helix is replaced with a beta hairpin ! 3 helices; folded leaf, opened
17053 ! CA-atoms only
17061 ! engineered cro monomer bound nonspecifically to DNA
17054 ! monomeric insertion mutant
17056 ! insertion mutant k56-[dgevk]-f58w
17060 ! insertion mutant k56-[dgevk]
105139 !SQ P09964
17064 ! CASP3
108035 !SQ Q8VL32 
47435 ! probably does not bind to DNA
17074 ! CASP3
47438 ! lacks the first helix of canonical fold ! 3 helices; bundle, partly opened, right-handed twist
109813 ! contains extra C-terminal all-alpha dimerization subdomain; the dimer may bind DNA
105255 !SQ Q8ZPR1 # ! Structural genomics target
47445 ! 4 helices; orthogonal array
79046 ! a part of a ternary s-domain complex
47453 ! 4 helices; the long C-terminal helix protrudes from the domain and binds to DNA
71999 ! 3-helical fragment
47458 ! 4-helices; bundle, closed, left-handed twist; 2 crossover connections
47459 ! dimer of two identical helix-loop-helix subunits
47461 ! BHLHZ region; contains leucine-zipper motif
80576 ! complexed with Myc
80636 ! complexed with Mad
81751 ! BHLHZ region; contains leucine-zipper motif
80575 ! complexed with Max
81753 ! BHLHZ region; contains leucine-zipper motif
80635 ! complexed with Max
99498 ! complexed with importin-beta
95469 ! fused interacting segments 
47472 ! core: 4 helices; array of 2 hairpins, opened
47473 ! Duplication: consists of two EF-hand units: each is made of two helices connected with calcium-binding loop
47474 ! made of two EF-hands only
104623 !SQ P02633 ! calbindomodulin; re-engineered to undergo a conformational opening
61253 ! EF-hand swapped dimer
47478 ! dimer: subunits are made of two EF-hands
81754 ! MTS1 protein
68057 ! apo-form
79585 ! complex with high-affinity target peptide trtk-12, chains X and Y
17166 ! complex with the C-terminal negative regulatory domain of p53
95080 ! complexed with a peptide from Ndr kinase, chains C and D
79393 ! complex with high-affinity target peptide trtk-12, chains C and D
47484 ! ligand of annexin II
17185 ! complex with annexin I N-terminus
47487 ! Migration inhibitory factor-related protein 8
70371 ! structure in a hexameric form
89048 ! calcium-binding pollen allergen; two EF-hands per subunit
84349 ! EF-hand swapped homodimer
90608 ! monomeric solution structure
104198 !SQ Q84V36
47489 ! 5 helices; two EF-hands plus one of additional helices in the N-terminal part
17190 ! this domain only
47492 ! 6-helices; array of 3 hairpins, closed ! made with two-helical hairpin and two EF-hands
65121 ! without the N-terminal alpha-hairpin
105249 !SQ P02625
104964 !SQ P20472
104965 !SQ P20472
47502 ! Duplication: made with two pairs of EF-hands
17227 ! calcium-saturated N-terminal domain
17233 ! fragment, corresponding to the 3rd EF-hand
17231 ! fragment, corresponding to the 3rd EF-hand
17234 ! N-domain only
17236 ! N-domain only
17245 ! N-domain only
77864 ! calcium saturated troponin C bound to troponin I
17243 ! N-domain only
17241 ! C-domain only; N-terminal domain is in 2CTN
17242 ! N-domain only; C-terminal domain is in 3CTN
62862 ! C-domain only
85983 ! calcium saturated troponin C bound to troponin I fragment, chain B
17239 ! heterodimer of 3rd and 4th EF-hands
17238 ! N-domain only
17240 ! N-domain only
17247 ! N-terminal domain of two EF-hands
17248 ! 4-calcium form
17249 ! 4-calcium form
17250 ! calcium-saturated form
17251 ! complexed with a 47 residue (1-47) fragment of troponin I
17252 ! C-domain only
93857 ! N-domain only; complexed with a troponin I fragment; chain B
66140 ! C-domain only
17254 ! N-domain only
78292 ! N-domain only; complexed with a troponin I fragment
17255 ! N-domain only; complexed with a troponin I fragment
17253 ! N-domain only
104822 !SQ Q7ZZB9 1-89
104783 !SQ Q7ZZB9 1-89
104553 !SQ P04571
17262 ! C-terminal domain (w81-s161)
17261 ! C-terminal domain (w81-s161)
62700 ! defunct EF-hand; N-terminal domain only
62701 ! defunct EF-hand; N-terminal domain only
47512 ! structurally most similar to sarcoplasmic calcium-binding protein
101179 ! structurally most similar to sarcoplasmic calcium-binding protein
83761 ! complexed with Marcks calmodulin binding domain peptide, chain B
91054 ! complexed with a myristoylated peptide, chain B
17264 ! trifluoperazine 1:1 complex
105670 !SQ P02593
99022 ! N-terminal domain only
17270 ! complexed with calmodulin-binding domain of calmodulin-dependent protein kinase
17275 ! complexed with calmodulin-binding peptide from smooth muscle myosin light chain kinase
17276 ! trifluoperazine 1:2 complex
17281 ! N-terminal domain
60056 ! C-terminal domain
66415 ! N-terminal domain
66416 ! C-terminal domain
17282 ! C-terminal domain in calcium-loaded form
17283 ! C-terminal domain in apo form
17280 ! mutant, E84 deleted
80540 ! complexed with an endothelial nitric oxide synthase peptide, chains B, D, F and H
104635 !SQ P62161 ! apocalmodulin; oligomer with swapped EF-hand units
104640 !SQ P62161 ! apocalmodulin; oligomer with swapped EF-hand units
47520 ! mutant with a two residue deletion in the central helix
62643 ! complex with a ca2+/calmodulin dependent kinase kinase fragment
17289 ! C-terminal domain
86297 ! complex with the C-terminal fragment of glutamate decarboxylase, chains B and C
17294 ! complex with a fragment of the rat ca2+/calmodulin dependent protein kinase
17288 ! N-terminal domain
17295 ! complex with a binding peptide of the human Ca2+-pump
79645 ! complex with the target sequence of Calmodulin-dependent protein kinase I (1a06), chains E and F
87198 ! structural genomics
83244 ! N-terminal domain, apo form
83245 ! N-terminal domain, calcium bound form
104918 !SQ Q42478
84782 ! C-terminal domain
87319 ! complexed with the cdc31p-binding domain (peptide) from kar1p, chain B
81756 ! light chain of class V myosin
78598 ! complexed with iq2 fragment of a class V myosin myo2p, chain B
91558 ! complexed with iq2 and iq3 fragment of a class V myosin myo2p, chain C
78599 ! complexed with iq4 fragment of a class V myosin myo2p, chain B
105955 !SQ P13543
105265 !SQ P13543
105956 !SQ P07291
105266 !SQ P07291
47533 ! Calcium-myristoyl switch; only one EF-hand is functional
17328 ! myristoylated protein
98594 ! complexed with a kv4.2 peptide, chain B
105310 !SQ P28583 329-508
107014 !SQ Q9SRP5 2-67 # N-domain only
17335 ! first EH domain
17336 ! second EH domain
17339 ! second EH domain ! CASP3
17338 ! second EH domain
17337 ! third EH domain
62640 ! first EH domain
81758 ! 4 EF-hands assembled in a compact structure like the Penta-EF-hand proteins; contains additional N-terminal all-alpha subdomain
76748 ! Ca-free structure
47550 ! Calpain small subunit homologue
96547 ! mu-like isoform with the large and small subunits fused in a single chain
92280 ! complexed with calpastatin dic
92278 ! complexed with calpastatin inhibitory domain c (dic) and peptide inhibitor
96548 ! mu-like isoform with the large and small subunits fused in a single chain
17355 ! N-termini of both chains are disordered in the crystal structure
47559 ! probably lost calcium-binding function; contains extra helices in each domain
60736 ! EF-hands 3&4 complexed with Z-repeat 7 from titin, chain B
105820 !SQ Q02818 228-326
47565 ! the N-terminal extension, containing a few short helices, forms a flexible lid for the binding cavity
47571 ! duplication: consists of 2 similar domains composed of 2 EF hand-like motifs each
47575 ! core: 4 helices: bundle
47577 ! Pfam 00307
17395 ! CASP2
47580 ! tandem repeat of four CH domains ! duplication: consists of tandem repeat of two CH domains
104385 !SQ Q7G188 123-623
105095 !SQ O59945 108-614
17399 ! second CH domain
47584 ! duplication: consists of tandem repeat of two CH domains
89056 ! duplication: consists of tandem repeat of two CH domains
105546 !SQ Q9QXS1 182-411
105548 !SQ Q9QXS1 182-411
101194 ! member of rp/eb family 
108642 !SQ Q15691 2-132 # ! Structural genomics target
108377 !SQ Q61166 16-116 # ! Structural genomics target
104062 !SQ O14188 32-190
107900 !SQ P37804 23-153 # ! Structural genomics target
47586 ! core: 4 helices: bundle; unusual topology
47587 ! duplication: consists of 2 helix-loop-helix structural repeats
107903 !SQ P09874 661-1010
47591 ! core: 4 helices: open bundle; capped by two small 3-stranded beta-sheets ! duplication: consists of two structural repeats
47592 ! binds to the transactivation domain of human p53
47593 ! Pfam 02201
100276 ! structural genomics
100277 ! structural genomics
107852 !SQ Q61466 252-331 # ! Structural genomics target
81766 ! core: 4 helices: bundle; flanked by two short beta-hairpins ! duplication: consists of two structural repeats
106834 !SQ P28366
106830 !SQ P28366
47597 ! core: 4 helices; array of 2 hairpins, opened
47598 ! formerly Met repressor-like; dimeric proteins; the N-termini form a small beta-sheet ribbon
17446 ! myl mutant
85849 ! a mutant with 3(10) helices replacing a wild-type beta-ribbon
17454 ! includes 15 residues common with the tetramerization domain
100970 ! similar to the phage repressor family
47605 ! plasmid-encoded
100971 ! plasmid-encoded, similar to the phage repressor family
47615 ! core: 4 helices; bundle, closed, left-handed twist; right-handed superhelix
47616 ! this domains follows the thioredoxin-like N-terminal domain
17656 ! CA-atoms only
17660 ! CA-atoms only
83158 ! chimeric isozyme
104180 !SQ P08263
104184 !SQ P08263
104172 !SQ P08263
108003 !SQ P08263
104176 !SQ P08263
17719 ! fused with synthetic linker-c-terminal fibrinogen gamma chain fragment
107757 !SQ P08515
17721 ! fused with a gp41 epitope of HIV-1
17723 ! fused with ankyrin binding domain of alpha-Na,K-ATPase
47630 ! synonym: hematopoietic prostaglandin D synthase
89061 ! synonym: hematopoietic prostaglandin D synthase
107395 !SQ Q9NJQ6 # Fragment
63555 ! maleylacetoacetate isomerase
81355 ! formerly a part of class theta enzymes
17739 ! fused with nuclear matrix targeting signal of transcription factor AML-1
101210 ! cannot be assigned to any of the known GST classes
63557 ! similar to class zeta enzymes
47641 ! similar to class phi enzymes
69033 ! similar to class theta enzymes; the N-domain undergoes a redox-controlled structural transition
97594 ! oxidized form; N-domain adopts a different all-alpha dimeric fold
47643 ! 4 helices; bundle, left-handed twist; right-handed superhelix
101214 ! 4 helices; bundle, right-handed twist; right-handed superhelix
108300 !SQ Q79V62 174-278
106034 !SQ Q79V62 180-283 ! complexed with the KaiC C-terminal peptide (SQ Q79V60 488-518), chains C and D
106040 !SQ Q79V62 180-283 ! complexed with the KaiC C-terminal peptide (SQ Q79V60 488-518), chains C and D
101219 ! KaiA from Nostoc species lacks the N-terminal CheY-like domain
104849 !SQ Q79PF6 # structured linker 136-176 in swapped dimer
109836 ! forms a helix-swapped dimer that otherwise is similar to the KaiA domain dimer
109175 !SQ P40399 1-84
47654 ! 4 long helices; bundle, left-handed twist (coiled coil); right-handed superhelix
100016 ! three-helical fragment
100019 ! three-helical fragment
17770 ! three-helical fragment; similar to one spectrin repeat
17772 ! three-helical fragment; similar to one spectrin repeat
98739 ! three-helical fragment; similar to one spectrin repeat
74281 ! three-helical fragment; similar to one spectrin repeat
61236 ! three-helical fragment; similar to one spectrin repeat
109839 ! four-helical bundle without significant twist
105229 !SQ Q9JMX9
109843 ! the first three helices are longer than the fourth one and, taken separately, adopt a Spectrin repeat-like fold (scop_cf 46965)
105113 !SQ P05067 374-565 # extra N-terminal alpha-hairpin 
107107 !SQ P05067 460-569 # structures are known for other fragments: 28-123 (scop_sp 56494); 124-189 (scop_sp 89814); 287-344 (scop_sp 57371); 681-/-711 (scop_sp 58608)
47667 ! 4 helices; bundle, left-handed twist; left-handed superhelix
89063 ! 4 helices; bundle, right-handed twist; left-handed superhelix
85915 ! truncated variant
47680 ! 4 helices; irregular array
63561 ! core: 2 helices and adjacent loops
63562 ! the bacterial omega and eukaryotic RPB6 subunits both function in polymerase assembly; the common core is involved in conserved interactions with other subunits    
63563 ! 4 helices; irregular array
105790 !SQ Q8RQE7 #! part of multichain biological unit
55295 ! essential subunit of RNA polymerases I, II and III
101223 ! 4 helices; irregular array
89068 ! 4 helices; irregular array
47685 ! 4 helices; irregular array, disulfide-linked
47687 ! can be classified as disulfide-rich
17793 ! semisynthetic antagonist
47693 ! 4 helices; irregular array, disulfide-linked
81777 ! 4 helices; irregular array, disulfide-linked
81782 ! 4 helices; folded leaf; right-handed superhelix
81785 ! present only in a long splicing variant of DFF45; essential for chaperone activity
77478 ! CASP5
47698 ! 4 helices; folded leaf; right-handed superhelix
47699 ! can be classified as disulfide-rich
17809 ! complexed with prostaglandin b2
81787 ! different pattern for Cys-pairing compared with ns-LTP1
47715 ! two chains result from a single-chain precursor
105307 !SQ P23110
47718 ! core: 4 helices; bundle
47719 ! homotetramer
17829 ! true tetrameric structure can be generated from crystallographic symmetry ! independent NMR structures in other entries are somewhat different
17870 ! designed dimer
17864 ! mutant dimerisation domain with changed interaxial angle
69035 ! core: 4 long helices; bundle
69036 ! homotetramer
47723 ! 4 helices; bundle, partly opened
47724 ! this domain is the first in the fragment of known structure
47726 ! Single-stranded DNA-binding protein
47728 ! core: 4 helices; bundle, partly opened, capped with a beta-sheet
47729 ! dimer of identical subunits
88878 ! heterodimer of two related subunits
88880 ! heterodimer of two related subunits
91465 ! alpha2 isoform
63566 ! provisional classification awaiting the entire protein structure
47740 ! core: 4 helices, bundle
47741 ! contains 2Fe-2S cluster
108739 !SQ Q46509
105581 !SQ Q46509
108442 !SQ P80457
106373 !SQ P72223
47751 ! 4 helices; the three last helices form a bundle similar to that of the RuvA C-domain
47752 ! overall fold is similar to the fold of N-terminal subdomain of the GluRS anticodon-binding domain (1GLN)
47754 ! periplasmic protein that supports acid resistance in enteric bacteria
17927 ! CASP3
63569 ! 4 helices; an orthogonal array
84170 ! complexed with paip2 peptide, chain B
84171 ! complexed with paip1 peptide, chain B
47756 ! 4 helices; an orthogonal array
101232 ! 4 helices; up-and-down bundle; topological similarity to the bromodomain-like and SAM domain-like folds
47761 ! 4 helices; open up-and-down bundle; binds alpha-helical peptides
17930 ! complex with Mad1 peptide; chain B; CASP4
94514 ! complex with Mad1 peptide; chain B
105279 !SQ Q96ST3 295-383
105281 !SQ Q96ST3 295-383
17931 ! complex with Mad1 peptide; chain A
81789 ! 4 helices; open up-and-down bundle; flexible N-terminal tail
77269 ! deletion mutant
101237 ! 4 helices; array
93441 ! flexible linkers excluded
107183 !SQ P54725 230-288
104322 !SQ P54727 275-342 # structure of the N-terminal domain (1-87) is also known (scop_sp 102778)
109853 ! # core: 4 helices; bundle, closed, left-handed twist; an unusual topology with a higher contact order
109854 ! contains metal-binding site on the bundle surface surrounded by loops 
109855 ! probably distantly related to the DinB family (Pfam 05163)
105121 !SQ O31562
109858 ! 4 helices; dimer of identical alpha-hairpin subunits; open bundle
103987 !SQ Q8YNP7
47768 ! 4-5 helices; bundle of two orthogonally packed alpha-hairpins; involved in the interactions with DNA and proteins
17932 ! CASP3
106036 !SQ Q01842 42-118
106042 !SQ Q01842 42-118
106038 !SQ Q9I7G2 94-173
106079 !SQ Q00422 168-254 # structure of the Ets domain (320-429) is also known (scop_sp 46868)
106080 !SQ P11308 115-208
47781 ! duplication: contains two helix-hairpin-helix (HhH) motifs
47783 ! tetramer; binds Holliday junction
47787 ! duplication: consists of two RuvA-like domains (four HhH motifs); also contains a zinc-finger subdomain
47789 ! contains one classic and one pseudo HhH motifs
47794 ! contains one classic and one pseudo HhH motifs
95456 ! disordered in the other chains of this PDB entry
106186 !SQ P25454 81-395
106418 !SQ O73948
107752 !SQ P03003 352-419
47798 ! contains one classic and one pseudo HhH motifs
47802 ! contains one classic and one pseudo HhH motifs
47804 ! topologically similar to the second domain
18076 ! partly disordered
92385 ! one (lyase) domain only
81585 ! contains one classic and one pseudo HhH motifs
81584 ! topological similarity to the N-terminal domain
69045 ! includes the N-terminal heterodimerisation alpha-hairpin
47833 ! inserted in the phosphohistidine domain
98105 ! structural genomics
78718 ! CASP5
47835 ! 4-5 helices; right-handed superhelix
47836 ! the 5th, C-terminal helix is missing in some of the member structures
47838 ! topologically similar to one subunit in the interferon-gamma intertwined dimer
99756 ! myristoylated protein 
47842 ! the C-terminal helix region is disordered(?)
47845 ! the C-terminal helix region is missing(?)
47848 ! the C-terminal helix region is missing(?)
79321 ! the C-terminal helix region is missing
107854 !SQ O62708 7-98 # 73% sequence identity # ! Structural genomics target
101256 ! core: 5 helices; right-handed superhelix; swapped dimer with the two long C-terminal helices
105495 !SQ P14335 23-98
47851 ! 5 helices; array; two long helices form a hairpin that dimerizes into a 4-helical bundle
47856 ! 5 helices; bundle, closed, left-handed twist
47859 ! five-helical bundle ! probably related to four-helical (apo)lipoproteins
101261 ! 5 helices; bundle, closed, left-handed twist
101263 ! COG3404
101264 ! putative serine cycle enzyme
92498 ! structural genomics
109879 ! 5 helices; bundle, closed, left-handed twist; helices 2-5 adopt the Four-helical up-and-down bundle fold (scop_cf 47161)
105605 !SQ P26039 486-782 # 1SJ8 coverage; 1S7J coverage is 488-654
105606 !SQ P26039 486-782 # 1SJ8 coverage; 1S7J coverage is 488-654
109884 ! 5 helices; bundle, closed, left-handed twist 
109886 ! actin-binding motif that adopts different folds; possibly refolds upon binding 
109887 ! Hip1r thatch domain core
104722 !SQ O75146 773-965
109889 ! 4-helical bundle of the Bromodomain-like fold (scop_cf 47363); similar to helices 2-5 of the  Huntingtin interacting protein 12
105607 !SQ P26039 486-782 
47861 ! 5 helices; folded leaf, closed
47862 ! Lipid-binding can promote conformational changes and oligomerisation in some members
81806 ! the alternative subunit conformation is an open four-helical bundle; helices 3 and 4 form a contiguous helix
80120 ! the alternative subunit conformation
18140 ! CASP2
101267 ! pore-forming toxin
47866 ! circularly permuted saposin domain inserted in plant acid proteases
47871 ! cyclic peptide
18144 ! CASP4
47873 ! 5 helices; folded leaf, closed
47874 ! duplication: consists of four domains of the same fold
18146 ! domain 1 only
18158 ! with proline substitution by thioproline
47887 ! further duplication: consists of two four-domain units
74590 ! phosphorylation-mimicking mutant T356D
47894 ! 5 helices; folded leaf
47895 ! this domain interrupts the G-protein common fold
72626 ! bound to the goloco motif of rgs14, chains B and D
18213 ! species chimera
18216 ! species chimera
18221 ! species chimera
47911 ! 5 helices; irregular array; left-handed superhelix
18268 ! the polyproline region in this domain has been replaced by a short flexible linker
106649 !SQ P42768 241-309
47916 ! core: 4-5 helices; bundle; left-handed superhelix
108995 !SQ P19483
109014 !SQ P19483
109004 !SQ P00829
109023 !SQ P00829
47924 ! duplication: contains two similar domains of this fold
104440 !SQ P45568
104467 !SQ P45568
106266 !SQ P45568
106274 !SQ P45568
104455 !SQ P45568
104732 !SQ Q9X5F2
104744 !SQ Q9X5F2
47927 ! core: 5 helices; bundle
47932 ! 5 helices; bundle
18318 ! CASP4
94507 ! complexed with a snare peptide
94497 ! complexed with a snare peptide
94502 ! complexed with a snare peptide
47937 ! core: 5 helices; bundle
47942 ! core: 5 helices; bundle
18334 ! N-terminal domain only
94308 ! contains an upstream extension of gag p10 sequence, residues -28-0
47953 ! core: 5 helices; one helix is surrounded by the others
47954 ! duplication: consists of two domains of this fold
103963 !SQ P20248 175-432
108927 !SQ P20248 175-432
103969 !SQ P20248 175-432
103951 !SQ P20248 175-432
47970 ! contains an additional C-terminal helix
18389 ! domains A and B
79997 ! bound to the transactivation domain (peptide) of E2F-2
18390 ! domain A
86705 ! domain A - chains A, C, E, G; domain B - chains B, D, F, H; complexed with E2F peptide, chains P, Q, R, S
69059 ! 5 helices; one helix is surrounded by the others
69064 ! core: 5 helices; one helix is surrounded by the others
80753 ! CASP5
107696 !SQ Q81J58 # ! Structural genomics target
47972 ! core: 5 helices; contains one more helix and a beta-hairpin outside the core
48018 ! core: 5 helices: bundle
48019 ! associated with N-terminal domain from the AAA+ family of P-loop hydrolases
48020 ! contains an extra helix
106081 !SQ P38630 295-696 # helical segment (667-696) together with unassigned C-terminal sequence forms an all-alpha subdomain  
106083 !SQ P40339
106085 !SQ P38629
106087 !SQ P40348
106089 !SQ P38251
81632 ! core: 5-helical bundle; up-and-down; right-handed twist
81631 ! this domain follows the catalytic nucleotidyltransferase domain 
104548 !SQ P25500 18-497
104545 !SQ P25500 18-497
106871 !SQ O28126
106883 !SQ O28126
106136 !SQ O28126
69069 ! core: 5 helices: orthogonal array
107119 !SQ P32267
89081 ! 5 helices: orthogonal array
109904 ! 5 helices: irregular array 
107822 !SQ Q8CH02 165-239 # ! Structural genomics target
109909 ! 5 helices; array; forms a tight dimer in crystals
109911 ! Despite the Pfam annotation, this family shows no topological similarity to the TPR repeat proteins  
104320 !SQ Q9JR91 # ! Structural genomics target
109914 ! core: 5 helices; orthogonal array; folding similarity to the TipA-S domain (1ny9)
109915 ! oligomerizes via extra N-terminal helix forming trimeric coil-coiled
105451 !SQ O07517 # ! Structural genomics target
109919 ! 5 helices; array; probable biological unit is a homodimer
108635 !SQ Q9LUJ3 # ! Structural genomics target
101277 ! 6 helices: bundle; left-handed twist, up-and-down topology
47978 ! 6 helices, homodimer of 3-helical domains
104086 !SQ P33120
69074 ! 6 helices, homodimer of 3-helical domains
69077 ! includes the long 'spinal' helix
101282 ! 6 helices, homodimer of 3-helical domains
101287 ! 6 helices, heterodimer of 3-helical domains
100601 ! L27n domain; complexed with L27 domain of Patj
100603 ! complexed with L27n domain of Pals-1
109924 ! dimer of 3-helical segments; consists of two subdomains: 4-helical bundle and coiled coil
108049 !SQ P43035 1-85
47985 ! 6 helices: closed bundle; greek-key; internal pseudo twofold symmetry
47988 ! residues 334-418
47992 ! contains two domains of this superfamily: DED and DD, in this order
18438 ! complexed with Tube death domain
48005 ! complexed with Pelle death domain
81387 ! contains two domains of this superfamily: DED and DD, in this order
81818 ! DED is followed by an irregular C-terminal tail
48001 ! an inhibitor of interleukin-1beta generation
48007 ! core: 6 helices: closed bundle; greek-key; internal pseudo twofold symmetry
18443 ! CASP4
60828 ! complex with myristoyl-CoA
48012 ! 6 helices: bundle; one central helix is surrounded by 5 others
107526 !SQ Q9X286
107527 !SQ Q9X286
107524 !SQ Q9X286
107529 !SQ Q9X286
107525 !SQ Q9X286
96202 ! structural genomics
105912 !SQ P36929
105910 !SQ P36929
101306 ! core: 6 helices; bundle; one central helix is surrounded by 5 others
101308 ! DUF64: Pfam 01892 ! Pfam 01892; protein of unknown function DUF64
97414 ! structural genomics; MCSG target APC35681
107134 !SQ P54173 # ! Structural genomics target
48023 ! 6 helices: array
18455 ! CASP3
101311 ! 6 helices: orthogonal array
48033 ! irregular array of 6 short helices
104979 !SQ P51541
105424 !SQ P51541
48044 ! core: 6 helices; one central helix is surrounded by 5 others
101316 ! core: 6 helices; one central helix is surrounded by 5 others
97049 ! structural genomics
48049 ! 6 helices; bundle; one central helix is surrounded by 5 others
48052 ! Middle domain is all-alpha; C-terminal domain is immunoglobulin-like sandwich
48055 ! multihelical
48056 ! duplication: contains two structural repeats
48058 ! N-terminal domain is all-alpha; C-terminal domain is immunoglobulin-like sandwich
48064 ! multihelical; core: 5-helical bundle
48066 ! Pfam 00621
18516 ! autoinhibited
104960 !SQ  Q64096 624-958 # 98% sequence identity; note that the rat sequence Q63406 region 499-833 is 100% identical to the PDB sequence
103873 !SQ O75962 1231-1535
107422 !SQ Q9NZN5 766-1138
109513 !SQ Q9NZN5 766-1138
48075 ! multihelical; contains compact array of 6 short helices
81821 ! multihelical; irregular array of long and short helices
81826 ! multihelical; irregular array of long and short helices
48080 ! multihelical bundle; contains buried central helix
48082 ! C-terminal domain is all-alpha
101321 ! multihelical; contains two buried central helices
101323 ! pfam 04356: protein of unknown function (DUF489)
105437 !SQ P25746 # ! Structural genomics target
96613 ! structural genomics
48091 ! multihelical; can be divided into two subdomains
48096 ! multihelical; consists of two all-alpha subdomains ! contains a 4-helical bundle with left-handed twist and up-and-down topology
18549 ! Complex with a samp repeat from apc; chain B
62119 ! N-terminal RGS domain
63586 ! contains extra helices in the C-terminal extension
81831 ! multihelical; consists of two all-alpha subdomains each containing a 3-helical bundle with right-handed twist
81833 ! C-terminal part of Pfam 05364
104821 !SQ Q9KIZ2
104869 !SQ Q9KIZ2
74747 ! multihelical; consists of two all-alpha subdomains; contains a 4-helical bundle with left-handed twist and up-and-down topology
101326 ! multihelical; consists of two tightly associated 3-helical bundles with different twists
90725 ! structural genomics
101331 ! multihelical; consists of two all-alpha subdomains; dimer
48107 ! multihelical; consists of two all-alpha subdomains ! possible duplication: subdomains have similar topologies
106325 !SQ P00968
48112 ! multihelical; consists of two all-alpha domains
77473 ! mesopone state
105844 !SQ P00431
73156 ! proposed electron transfer pathway excised to form a ligand binding channel
73157 ! proposed electron transfer pathway excised to form a ligand binding channel
71632 ! engineered calcium-binding loop
106008 !SQ P00431
68852 ! engineered calcium-binding site
59406 ! Laue diffraction study on the structure of compound I
18604 ! manganese-binding mutant
107706 !SQ P00431
107710 !SQ P00431
108205 !SQ Q43758
101336 ! chloroplastic isoform
74753 ! duplication: tandem repeat of two CCP-like domains
74754 ! only the N-terminal CCP-like domain binds heme
105600 !SQ Q08129
48136 ! contains EGF-like module
107697 !SQ P05979 32-584
48139 ! multihelical; consists of two different 3-helical domains connected by a long, partly helical linker
105335 !SQ P14119
89094 ! multihelical; consists of two different alpha-helical bundles (4-helical and 3-helical)
85670 ! structural genomics
109603 ! multihelical; consists of two different alpha-helical bundles 
101340 ! Pfam 01966; metal dependent phosphohydrolases
48548 ! multihelical; can be divided into three subdomains ! 3',5'-cyclic-nucleotide phosphodiesterase, Pfam 00233
106736 !SQ Q07343 335-657
106742 !SQ Q08499 389-713
106740 !SQ Q08499 389-713
106743 !SQ O76074 534-858
106727 !SQ O76074 534-858
106725 !SQ O76074 534-858
107851 !SQ O76074 537-860
106745 !SQ O76083 241-566
106734 !SQ Q01064 126-482
101343 ! multihelical; consists of two different alpha-helical bundles 
48144 ! multihelical; consists of two different all-alpha subdomains, 4 helices each
48145 ! superficially similar to membrane translocation domains
48147 ! bifunctional membrane/RNA-binding protein
48149 ! multihelical; consists of two all-alpha domains
109339 !SQ P17802 1-225
109338 !SQ P17802 1-225
109337 !SQ P17802 1-225
104331 !SQ P04395
78285 ! borohydride trapped intermediate
78283 ! borohydride trapped intermediate
76723 ! borohydride trapped intermediate complex
78281 ! borohydride trapped intermediate
48162 ! multihelical; consists of two all-alpha domains
101352 ! multihelical; consists of two all-alpha subdomains
48167 ! multihelical consists of two all-alpha subdomains ! subdomain 1 (residues 10-100) is a 4-helical bundle
104131 !SQ Q08698
104129 !SQ Q08698
104127 !SQ Q08698
104133 !SQ Q08698
81836 ! multihelical, complex architecture
48172 ! multihelical; consists of two all-alpha subdomains
48175 ! N-terminal domain is alpha/beta and binds a light-harvesting cofactor
71280 ! complexed with thymine
107638 !SQ Q43125 13-497
107636 !SQ Q43125 13-497
48178 ! multihelical; common core is formed around two long antiparallel helices related by (pseudo) twofold symmetry
48179 ! N-terminal domain is Rossmann-fold with a family-specific C-terminal extension
48180 ! Hydroxyisobutyrate dehydrogenase domain is similar to one structural repeat in the 6-phosphogluconate dehydrogenase domain
101357 ! forms similar dimeric and tetrameric structures to the 6-phosphogluconate dehydrogenase domain and its dimer, respectively
90831 ! structural genomics
48181 ! duplication; contains two structural repeats
48185 ! duplication; contains two structural repeats swapped to fold into a figure eight knot
48188 ! Dimer of 5-helical motifs; similar to duplicated motifs of 6PGD and KARI
109949 ! duplication: contains two repeats of this domain 
109255 !SQ P28793
109279 !SQ P28793
109267 !SQ P28793
89103 ! forms segment-swapped dimer, unlike the homologous UDPGDH domain
48200 ! multihelical
48201 ! disulfide-linked dimer of two identical chains, 4 helices in each
101359 ! forms heterodimer with Fel d I-B chain
95136 ! fused with Fel d I-B
101361 ! forms heterodimer with Fel d I-A chain
95137 ! fused with Fel d I-A
48207 ! multihelical; up to seven alpha-hairpins are arranged in closed circular array; there may be sequence similarities between different superfamilies
81846 ! contains only the catalytic module, which interacts with the substrate
76739 ! complex with cellobiose
89105 ! cold-adapted family 8 xylanase
89107 ! endoglucanase 9G
48218 ! the other, N-terminal, domain is immunoglobulin-like
63588 ! overall domain organization is similar to Bacterial glucoamylase
63589 ! includes alpha-helical linker to the N-terminal domain and a small C-terminal beta-sandwich subdomain
108411 !SQ Q76IQ9
108409 !SQ Q76IQ9
108413 !SQ Q76IQ9
81850 ! overall domain organization is similar to Lactobacillus maltose phosphorylase
89108 ! unknown function; weak sequence similarity to the catalytic domain of cellulases
85548 ! structural genomics
108518 !SQ Q9RC92
48230 ! incomplete toroid
48235 ! Chondroitin AC lyase
109168 !SQ Q54873 287-1007
69089 ! preceded by a small all-beta Ig-like domain
89113 ! domain 2; preceded by a beta-domain of the galactose-binding domain-like fold
81854 ! incomplete toroid made of four hairpins
104830 !SQ Q9X592
48240 ! incomplete toroid made of four hairpins
48243 ! consists of two toroid domains: one of six and one of five hairpins
18866 ! complex with K-ras4b peptide substrate
77641 ! complex with k-ras4b peptide product
77639 ! complex with k-ras4b peptide product and farnesyl diphosphate substrate bound simultaneously
105405 !SQ Q02293
105298 !SQ P53610
18869 ! complex with k-ras4b peptide substrate and FPP analog
105286 !SQ P49356
105403 !SQ P49356
48251 ! probably related to other families, but has no known enzymatic activity
18875 ! N-terminally truncated fragment
18879 ! N-terminally truncated fragment
48255 ! multihelical; consists of two all-alpha domains
48257 ! duplication: large domain consists of two structural repeats ! the second repeat is interrupted by the small domain
48262 ! Cold-active enzyme
104040 !SQ P00891
104038 !SQ P00891
48263 ! multihelical
106654 !SQ P00183
106650 !SQ P00183
106656 !SQ P00183
106652 !SQ P00183
105759 !SQ P14779
105763 !SQ P14779
18965 ! CASP1
107578 !SQ P77901 
81863 ! implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis
101371 ! implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis
79977 ! atomic resolution structure
81867 ! functionalizes macrolide ring systems
81869 ! thermostable P450
48278 ! thermophilic P450
107781 !SQ Q972I2 # ! Structural genomics target
106026 !SQ P00178
104878 !SQ P11712
107238 !SQ P08684
108987 !SQ P08684
108988 !SQ P08684
108986 !SQ P08684
63591 ! multihelical; forms intertwined dimer of identical 5-helical subunits
63593 ! contains an HTH motif
48299 ! multihelical; intertwined tetramer
97772 ! dimeric solution structure, similar to the SinR repressor dimerisation domain-like fold
97775 ! includes hinge region 33-51 that is flexible in both chains
97779 ! includes hinge region 33-51 that adopts a helical conformation in chain A but is flexible in chain B
48304 ! multihelical; intertwined trimer of identical 3-helical subunits
48309 ! multihelical; consists of two all-alpha domains
48316 ! multihelical; core: 5-helical bundle; binds cofactor at the beginning of third helix
48321 ! contains one core bundle; forms dimer
48325 ! duplication: contains two core bundles arranged as in the other family dimer
81871 ! multihelical; contains a 3-helical bundle surrounded by several shorter helices
79153 ! complexed with human Dss1 fragment, chain B
79193 ! complexed with human Dss1 fragment, chain B
76953 ! complexed with human Dss1 fragment, chains A and C
81877 ! multihelical; contains a 3-helical Hin recombinase-like subdomain and two long dimerisation helices
79194 ! this domain is partly disordered in the crystal structure
76954 ! this domain is poorly ordered in the crystal structure
81274 ! multihelical oligomeric protein; structure of whole subunit is not known yet but are probably composed of three different domains
81273 ! available NMR structures suggest two very different dimerisation modes of the N-terminal domain
80536 ! N-terminal, dimerisation domain; res. 1-46
78155 ! N-terminal, dimerisation domain; res. 1-57
17895 ! C-terminal DNA-binding domain; res. 90-136
17896 ! C-terminal DNA-binding domain; res. 90-136
93592 ! N-terminal, dimerisation domain; res. 1-50; this crystal structure displays dimerisation mode similar to the 1ni8 solution structure
88945 ! multihelical; consists of a conserved 4-helical core and a variable insert subdomain
19068 ! sigma2 domain only with a large insert subdomain
105793 !SQ Q9WX78 
76640 ! truncated sigma2 domain core; anti-sigma factor binding domain
48333 ! multihelical; consists of 2 all-alpha subdomains
19070 ! CASP4
109222 !SQ P23909 2-800
81885 ! multihelical; consists of 2 all-alpha subdomains
106835 !SQ P28366
106831 !SQ P28366
101385 ! multihelical; consists of 2 all-alpha subdomains, "rigid" one and "mobile" one
109141 !SQ Q9PMK9
101390 ! multihelical; consists of 2 all-alpha subdomains connected by a long helix
89123 ! multihelical; array of longer and shorter helices; contains an alpha-hairpin dimerisation subdomain
89125 ! putative snoRNA binding domain
89126 ! also contains an N-terminal, fibrillarin-binding alpha+beta subdomain
89127 ! AF2088
86150 ! structural genomics; complex with fibrillarin (AF20087)
48339 ! multihelical; bundle of longer and shorter helices
48344 ! multihelical; three-helical bundle in the core is surrounded by non-conserved helices
48345 ! this domain is interrupted by a jelly-roll beta-sandwich domain
101398 ! multihelical; consists of two subdomains
48349 ! multihelical
48358 ! GTPase regulator associated with focal adhesion kinase
48365 ! multihelical
63599 ! multihelical; can be divided into an alpha-alpha superhelix domain and a long alpha-hairpin dimerization domain
81890 ! multihelical; can be divided into three subdomains (neck, body and tail)
81891 ! the neck subdomain is an alpha-alpha superhelix; the tail subdomain is similar to the RuvA C-terminal domain-like
81892 ! the 'neck' domain corresponds to the C-terminal part of Pfam 01743
87447 ! the tail subdomain is not present in this structure
108572 !SQ O66728 443-824 # chain B coverage
48370 ! multihelical; 2 (curved) layers: alpha/alpha; right-handed superhelix
78399 ! complex with ICAT
67044 ! complex with apc beta-catenin binding repeat
66549 ! complex with htcf-4
19115 ! complex with xtcf3-cbd
96618 ! complex with beta-catenin binding domain of axin, chain B
78225 ! complex with ICAT
106906 !SQ P35222 145-664 ! complex with a phosphorylated apc 20aa repeat fragment (SQ P25054 1468-1529), chains C and D
67061 ! complex with htcf-4
95606 ! complexed with a phosphorylated sv40 cn peptide, chains A and B 
94764 ! complexed with a bipartite NLS peptide, chain A 
94765 ! complexed with a bipartite NLS peptide, chain A 
95607 ! complexed with a non-phosphorylated sv40 cn peptide, chains A and B 
66260 ! complexed with autoinhibitory peptide
92576 ! bound to five fxfg repeats from yeast nsp1p, chains D, E and F
86637 ! bound to a glfg nucleoporin peptide, chains C, D, E and F
99494 ! complexed with SREBP-2 HLH domain 
78653 ! bound to the non-classical nls(67-94) of pthrp, chain Q
99642 ! complexed with a nup2p N-terminal fragment, chains C and D
100908 ! duplication: family members contains 2 or more structurally similar domains of this fold connected by unstructured linkers  
19137 ! middle domain
94413 ! C-terminal domain
63606 ! contains three domains of this fold connected with long linkers
89129 ! pseudo-HEAT repeat
99758 ! complexed with a C-terminal peptide of strad, chain B
105941 !SQ P09960 
99916 ! single alpha-hairpin repeat
19140 ! single alpha-hairpin repeat
19142 ! single alpha-hairpin repeat
48397 ! contains a FeS4 centre
101410 ! Pfam 03130
106794 !SQ O26289
106195 !SQ Q81BA8
109968 ! N-terminal part of Pfam 06272
105132 !SQ Q9UBQ5
85458 ! complexed with bromo-dodecanol
85456 ! complexed with bromo-dodecanol
97318 ! complexed with ARF1
81902 ! Helicobacter Cysteine-rich Protein
81903 ! a penicillin-binding protein
77440 ! structural genomics
19185 ! complex with K-ras4b peptide substrate
77640 ! complex with k-ras4b peptide product
77638 ! complex with k-ras4b peptide product and farnesyl diphosphate substrate bound simultaneously
105404 !SQ Q04631
105297 !SQ Q04631
19188 ! complex with k-ras4b peptide substrate and FPP analog
105285 !SQ P49354 
105402 !SQ P49354
19199 ! bound to ps-raf259 peptide
19201 ! bound to r18 peptide
19203 ! phosphopeptide complex
19205 ! phosphopeptide complex
62136 ! complexed to serotonin N-acetyltransferase
86689 ! complex with a proton ATPase peptide, chain P
86691 ! complex with a proton ATPase peptide, chain P
19208 ! TPR1-domain
19209 ! TPR2-domain
19213 ! complexed with the pts1 peptide
62451 ! truncated form(?); adopts a different fold
81908 ! a Fis1p-like and Cgi-135 homologous domain
76947 ! structural genomics
104072 !SQ Q02790 145-427 # ! second FKPB domain
104667 !SQ Q02790 145-427 # ! second FKPB domain
109150 !SQ O15294 16-400
76434 ! complexed with Ins(1,4,5)P3
48469 ! protein involved in membrane trafficking and signal transduction
99458 ! complexed with beta-secretase C-terminal phosphopeptide 
71912 ! complexed with cation-independent M6PR C-terminal peptide
95318 ! complexed with beta-secretase C-terminal phosphopeptide 
99456 ! complexed with beta-secretase C-terminal phosphopeptide 
67325 ! complexed with peptide from cation-dependent mannose 6-phosphate receptor
73882 ! complexed with peptide from cation-independent mannose 6-phosphate receptor
67030 ! complexed with peptide from cation-independent mannose 6-phosphate receptor
90359 ! complex with inositol(4,5)p2
109975 ! found in proteins involved in regulation of nuclear pre-mRNA; some sequence similarity to VHS domain
106144 !SQ P39081 1-140
106141 !SQ P39081 1-140
74786 ! synonym: testis/brain RNA-binding protein, TB-RBP
48029 ! fragmented superhelix; consist of 3/4-helical motifs and connecting helices
18457 ! C-terminal domain only
73980 ! middle and C-terminal domains
100568 ! structural genomics
48483 ! multihelical ! large nearly all-alpha domain
48486 ! N-terminal domain is beta-sandwich similar to colipase-binding domain of pancreatic lipase ! contains alpha plus beta subdomain: res. 341-495; alpha-beta(5)-alpha
48492 ! multihelical; consists of two all-alpha subdomains
48497 ! multihelical; interlocked (homo)dimer
19248 ! class d; complex with 4-epi-tetracycline
104974 !SQ P23217
104617 !SQ P23217
104609 !SQ P23217
105043 !SQ P23217
100723 ! structural genomics
97626 ! structural genomics
106429 !SQ P96222
109980 ! gamma-butyrolactone receptor
107859 !SQ O66122
107863 !SQ O66122
106298 !SQ Q8ZQN9 # ! Structural genomics target
105540 !SQ P42105
81384 ! multihelical; interlocked heterodimer with F-box proteins
81910 ! Suppressor of kinetochore protein 1,Scskp1
81385 ! multihelical; interlocked heterodimer with the Skp1 dimerisation domain
48507 ! multihelical; 3 layers or orthogonally packed helices
79499 ! complexed with co-activator peptide
79707 ! complexed with co-activator peptide
79498 ! complexed with co-activator peptide
19276 ! complex with 9-cis retinoic acid
68251 ! heterodimer with PPAR-gamma complexed with co-activator peptides
107849 !SQ P28702 298-528
84769 ! complexed with coactivator peptide, chains B and E
87989 ! complexed with coactivator peptide, chains E, F, G and H
105945 !SQ P06401 682-932
105958 !SQ P06401 679-929
19292 ! complex with 4-hydroxytamoxifen
19294 ! complex with diethylstilbestrol and a peptide
19295 ! complex with estradiol
76367 ! complex with raloxifene core and TIF2 NRbox2 peptide; chains C and D
76369 ! complex with 17beta-oestradiol and TIF2 NRbox3 peptide; chains C and D
19308 ! complex with estradiol
19309 ! complex with partial agonist genistein
80415 ! complex with selective triazine modulator
19310 ! complex with antagonist raloxifene
106635 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
106626 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
106625 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
106638 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
106619 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
106613 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
106618 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
106612 !SQ O97775 661-910 # 100% sequence identity to human sequence (SQ P10275 669-918)
71121 ! complex with the agonist AZ 242
68271 ! complexed with a co-activator peptide
68682 ! complexed with an antagonist and a SMRT corepressor peptide
109404 !SQ P37231 232-505
68252 ! heterodimer with RXR-alpha complexed with co-activator peptides
71126 ! complex with the agonist AZ 242
92092 ! complexed with an src-1 coactivator peptide and sr12813
48534 ! the ortholog of RXRs in insects
92047 ! complexed with a co-activator peptide, chain B
91618 ! complexed with a co-activator peptide, chain B
105389 !SQ O75454 233-447
105387 !SQ O75454 233-447
106851 !SQ O75454 233-458
77547 ! complexed with a co-activator peptide
108630 !SQ O75454 233-447
104393 !SQ P41235 139-369
87942 ! complexed with a co-activator peptide, chains C and D
93501 ! complexed with a co-activator peptide, chains C, D and E
93506 ! complexed with a co-activator peptide, chains C, D and E
107850 !SQ Q13133 207-445
109537 !SQ P11474 289-516 
48536 ! multihelical
48537 ! duplication: all chain but the N-terminal helix forms two structural repeats
109992 ! multihelical; consist of two subdomains
107439 !SQ Q9UJ41
109997 ! multihelical; open array
109999 ! includes the upstream linker region not covered by the Pfam model
109088 !SQ P22257
106239 !SQ Q9KQS5
110003 ! multihelical; 2 layers or orthogonally packed helices 
106075 !SQ Q9NZD2
106078 !SQ Q9NZD2
110008 ! multihelical bundle; contains buried central helix 
107150 !SQ P47596 # ! Structural genomics target
110013 ! multihelical; consists of two topologically similar alpha-helical bundles
106158 !SQ P34704
110018 ! multihelical; consists of 2 four-helical bundles
105027 !SQ Q03103 56-424 #  similar active site architecture to scop_sf 69000
105047 !SQ Q03103 56-424 #  similar active site architecture to scop_sf 69000
48551 ! multihelical; one domain consists of two similar disulfide-linked subdomains
48554 ! duplication: consists of three domains of this fold
106824 !SQ P02768 29-596
69111 ! domain 3 lacks the last subdomain
73162 ! complexed with skeletal actin
48556 ! multihelical, consists of three all-alpha domains
107061 !SQ P24058
107057 !SQ P24058
107053 !SQ P24058
104914 !SQ Q88N37
101446 ! multihelical, consists of three all-alpha domains
48575 ! multihelical; core: 8 helices (C-J) are arranged in 2 parallel layers
48576 ! duplication: two metal-binding sites are related by a pseudo dyad that also relates helices C-F to helices G-J
108601 !SQ Q9X1M1
108600 !SQ Q9X1M1
108605 !SQ Q9X1M1
108604 !SQ Q9X1M1
108603 !SQ Q9X1M1
48581 ! synonym: Farnesyl diphosphate farnesyltransferase
48591 ! multihelical; 8 helices arranged in 2 parallel layers
48592 ! duplication: two 4-helical subdomains are related by a pseudo dyad passing through the ATP-binding site
109327 !SQ P61491
109379 !SQ P61491
89154 ! multihelical; bundle
89157 ! segment-swapped dimer
105390 !SQ Q8ZPK0 # ! Structural genomics target
48599 ! multihelical; core: 6 helices, bundle
48601 ! intertwined homodimer of 3-helical subunits
19493 ! CASP1
48604 ! duplication: 2 weak structural repeats resembling subunits of E. coli protein
48607 ! multihelical: forms a boat-shaped protein shell around cofactors
48608 ! duplication: consists of two 8-helical repeats
48610 ! soluble light harvesting protein
19507 ! CASP2
48612 ! multihelical; bundle
48613 ! duplication: contains two structural repeats of 3-helical motif
85737 ! heme-free structure
105153 !SQ P09601
105367 !SQ P09601 10-223
106464 !SQ P09601
108622 !SQ P06762 11-222
107941 !SQ P06762 11-222
108434 !SQ P71119
63628 ! gram-negative bacterial heme oxygenase/iron-starvation protein
105671 !SQ O69002
101458 ! Pfam 03070; HO-related family lacking the heme-binding site
97826 ! structural genomics; NESG target PRF34
95806 ! structural genomics
107779 !SQ O58873
107173 !SQ P25052
107461 !SQ P25052
101463 ! Pfam 05312
101466 ! contains a di-iron centre similar to that of the ferritin-like superfamily
69117 ! multihelical; contains 4-helical bundle and 2-helical arm
69118 ! probable biological unit contains six domains of this fold arranged with 32 symmetry
101468 ! hexamer of single domain subunits
108655 !SQ Q9X1V5 # ! Structural genomics target
94359 ! structural genomics; MCSG target APC4843
69119 ! duplication: two-domain subunits form a helix-swapped trimer
69120 ! a novel enzyme with thioredoxin-like activity
81922 ! multihelical; array
81923 ! duplication: contains two structural repeats of 4-helical motif
79093 ! complex with ClpS
104818 !SQ Q83LR6
78313 ! complex with ClpS
81929 ! multihelical; array
81930 ! duplication: contains four structural repeats arranged into two intertwined 4-helical subdomains
101472 ! multihelical; bundle
101475 ! eight-helical up-and-down barrel with a central ligand-binding cavity
101477 ! multihelical; bundle
101479 ! Pfam 03747
89161 ! multihelical; bundle
89162 ! duplication: contains two structural repeats of four helices each
81934 ! multihelical; array
81937 ! includes the N-terminal swapping arm made of three helices; possible DNA-binding function
48618 ! common core: 2 helices, disulfide-linked, and a calcium-binding loop
87491 ! zinc containing heterodimer of two different isoforms
87492 ! zinc containing heterodimer of two different isoforms
89169 ! heterodimer of two different isoforms
98592 ! heterodimer of two different isoforms
84960 ! zinc containing heterodimer of two different isoforms
89170 ! heterodimer of two different isoforms
98593 ! heterodimer of two different isoforms
84961 ! zinc containing heterodimer of two different isoforms
91261 ! complexed with a designed peptide inhibitor
93714 ! complexed with aspirin
106771 !SQ P60045 8-126 # ! yet another isoform, 98% identity
84963 ! possibly another isoform with isoleucine at second position
19552 ! complexed with vitamin E
107073 !SQ P59071
107015 !SQ P59071 ! different isoforms
107049 !SQ P59071
106888 !SQ P59071
106907 !SQ P59071
107026 !SQ P59071
106925 !SQ P59071
106889 !SQ P59071
106786 !SQ P59071
70148 ! complexed with aristolochic acid
72845 ! complexed with vitamin E
77150 ! complexed with a designed peptide inhibitor, chain P
106900 !SQ P59071
77148 ! complexed with a designed peptide inhibitor, chain P
107182 !SQ P59071
48631 ! presynaptic neurotoxic phospholipase A2
48632 ! neurotoxic phospholipase a2
48634 ! anticoagulant class II phospholipase A2
66867 ! complex with catalytic subunit
19560 ! complex with catalytic subunit
66868 ! complex with inhibitory subunit
19561 ! complex with inhibitory subunit
93433 ! complex with catalytic subunit
93434 ! complex with inhibitory subunit
107674 !SQ Q6SLM1 # fragment
83267 ! trimeric isoform
106758 !SQ Q9DF52 28-145 # ! 74% sequence identity
74796 ! monomeric Lys-49 phospholipase A2 homologue
99630 ! acidic, non-myotoxic phospholipase A2
48645 ! Monomeric Lys-49 phospholipase A2 homologue
69123 ! Asp-49 phospholipase A2 homologue
104098 !SQ Q9IAT9
104108 !SQ Q9IAT9 [Fragment]
104081 !SQ Q8JFB2 # 65% sequence identity
104048 !SQ Q8JFB2 # 65% sequence identity
108688 !SQ P00593
74797 ! group X secretory phospholipase A2
84728 ! atomic resolution structure
77479 ! Calcium-bound form
48646 ! 5 helices: irregular disulfide-linked array; also contains a small beta-hairpin
74223 ! complexed with cholesterol
19618 ! engineered beta-cryptogein complexed with ergosterol
19619 ! CASP2
48651 ! 5 helices: irregular disulfide-linked array; form homodimer
110034 ! 5 helices: irregular disulfide-linked array; topological similarity to the Fungal elicitin fold (scop_cf 48646)
104554 !SQ Q62997 239-346
48656 ! 6 helices: irregular non-globular array; also contains two small b-hairpins
69124 ! 3 helices, non-globular array; forms interlocked heterodimers with its targets
69125 ! not a true superfamily
68383 ! complex with ACTR domain
66773 ! free form
68382 ! complex with CBP/p300 ibid domain
101488 ! 5 helices, non-globular array; wraps around the N-terminal tail of its target
101489 ! not a true superfamily
48661 ! not a true fold
48662 ! interrupted alpha-helix
48666 ! consists of single alpha-helix and irregular N-terminal tail
48670 ! long alpha-helix interrupted in the middle
48676 ! string of short helices wrapped around the larger subunit
48680 ! string of short helices masking the FERM domain surface
60758 ! disordered
101494 ! single long helix crosslinking four tubulin subunits
48694 ! variable number of helices and little beta structure; not a true fold
48695 ! duplication: contains multiple CxxCH motifs
48697 ! contains four heme groups
74804 ! disulfide-crosslinked dimer
48702 ! synonym: <i>Desulfovibrio desulfuricans</i> Norway
48703 ! contains three heme groups; deletion of one of Cyt c3 heme-binding sites
105114 !SQ Q74BP5
48705 ! tandem repeat of two cytochrome c3-like domains with additional heme-binding site in the domain interface
81940 ! tandem repeat of four cytochrome c3-like domains
48707 ! consists of four heme-binding repeats
48711 ! the main characteristic feature of this motif is the packing of its two hemes ! many members contains one or more complete motifs flanked by incomplete motifs and/or other domains
48712 ! contains 3 complete motifs
48714 ! contains 1 complete motif
19683 ! CASP3
105866 !SQ Q8E9W8 # SO4144
48725 ! sandwich; 7 strands in 2 sheets; greek-key ! some members of the fold have additional strands
88519 ! VL-kappa domains of human and mouse antibodies are clustered by the sequence similarity within the germline encoded segment and then by the size of the complementarity determining regions CDR1 and CDR2, so the clusters may correspond to putative germline families in the species genomes; VL-kappa domains with artificial or grafted exogenous CDRs are listed as engineered species
20519 ! VL dimer of Bence-Jones protein REI
20531 ! VL dimer of Bence-Jones protein WAT
98135 ! part of anti HIV-1 gp120-reactive Fab 48D
98160 ! part of anti HIV-1 gp120-reactive Fab 412D
20534 ! VL dimer of Bence-Jones protein BRE
20094 ! part of humanized Fab TR1.9
20537 ! VL dimer of Bence-Jones protein BRE
67344 ! part of an anti-blood group A Fv
20543 ! VL dimer of Bence-Jones protein BRE
20521 ! VL dimer of Bence-Jones protein REI
19826 ! part of IgM Fv POT
19828 ! part of IgM Fv MEZ
19810 ! part of Fab 3D6
20604 ! part of Bence-Jones protein DEL
20446 ! part of IgM RF 2A2
76159 ! VL of anti-ferritin antibody
60987 ! part of IgM RF 2A2
98194 ! part of anti HIV-1 gp120-reactive Fab 47E
20522 ! VL of Bence-Jones protein REI; disulfide-free mutant
20545 ! VL dimer of Bence-Jones protein LEN
20547 ! VL dimer of Bence-Jones protein LEN
20548 ! VL dimer of Bence-Jones protein LEN
20550 ! VL dimer of Bence-Jones protein LEN
59435 ! VL dimer of Bence-Jones protein REC
20551 ! VL dimer of Bence-Jones protein LEN
20552 ! VL dimer of Bence-Jones protein LEN
20553 ! VL dimer of Bence-Jones protein LEN
20555 ! VL dimer of Bence-Jones protein LEN
20556 ! VL dimer of Bence-Jones protein LEN
91534 ! part of an anti HIV-1 Fab
62644 ! part of Fab BO2C11 against the C2 domain of factor VIII
19832 ! part of Fab Kau cold agglutinin IgM
19836 ! part of Fab Kau cold agglutinin IgM
61447 ! part of intact IgG B12 antibody
97477 ! part of HIV-1 neutralizing Fab x5
98141 ! part of anti HIV-1 gp120 Fab 17B
20262 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
98203 ! part of anti HIV-1 gp120 Fab 17B
20264 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
98210 ! part of anti HIV-1 gp120 Fab 17B
20266 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
91304 ! part of the esterolytic Fab ms6-164
85557 ! part of cationic cyclization catalytic Fab 4C6
97861 ! part of cationic cyclization catalytic Fab 4C6
97873 ! part of cationic cyclization catalytic Fab 4C6
20382 ! part of anti-dansyl Fv
97869 ! part of cationic cyclization catalytic Fab 4C6
20384 ! part of anti-dansyl Fv
97881 ! part of Diels-Alder catalytic Fab 13G5
91292 ! part of the esterolytic Fab ms6-164
96591 ! part of anti-cocaine Fab M82G2
96016 ! part of anti-cocaine Fab M82G2
85327 ! part of scFv 1695
97857 ! part of cationic cyclization catalytic Fab 4C6
66690 ! part of catalytic Fab 1D4
95401 ! part of Fab Sya/J6
20461 ! part of catalytic Fab 4B2
66694 ! part of catalytic Fab 1D4
97877 ! part of Diels-Alder catalytic Fab 13G5
97520 ! part of anti-cocaine Fab M82G2
20045 ! part of scFv trivalent antibody; N-terminal, VH domain is from B1-8 antibody (1A6U CH H); C-terminal, VL domain is from NQ11 antibody
20112 ! part of Fab 28B4
97865 ! part of cationic cyclization catalytic Fab 4C6
91300 ! part of the esterolytic Fab ms6-164
20430 ! part of anti-prion Fab 3F4
20142 ! part of Fab D2.3
20140 ! part of Fab D2.3
20240 ! part of Diels-Alder catalytic Fab 13G5
97374 ! part of anti-cocaine Fab M82G2
91283 ! part of the esterolytic Fab ms6-164
19904 ! part of Fab 4-4-20
72767 ! part of Fab D2.3
72762 ! part of Fab D2.3
20136 ! part of Fab MN14C11.6
20144 ! part of Fab D2.3
20166 ! part of hydrolytic antibody 6D9
97524 ! part of anti-cocaine Fab M82G2
20152 ! part of Fab D2.5
20154 ! part of Fab D2.5
59707 ! part of anti-IL2 Fab LNKB-2
20168 ! part of hydrolytic antibody 6D9
74125 ! part of retro Diels-Alder catalytic Fab 9D9
74117 ! part of retro Diels-Alder catalytic Fab 9D9
20160 ! part of Fv 4155
19902 ! part of Fab TE33
77801 ! part of anti-testosterone Fab 77
99145 ! part of blue fluorescent Fab 19G2
20146 ! part of Fab D2.3
20162 ! part of Fv 4155
20246 ! part of anticancer Fv B1; disulfide-stabilized
20114 ! part of Fab 28B4
91272 ! part of the esterolytic Fab ms6-164
77797 ! part of anti-testosterone Fab 77
91288 ! part of the esterolytic Fab ms6-164
20018 ! part of Fab Jel 103
20238 ! part of Diels-Alder catalytic Fab 1E9
20156 ! part of Fab D2.5
65015 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
20020 ! part of Fab Jel 103
20016 ! part of Fab Jel 103
19918 ! part of an anti-sweetener Fab
20304 ! part of catalytic Fab 33F12 with an aldolase activity
77347 ! part of anti-photoproduct Fab 64M-2
97853 ! part of cationic cyclization catalytic Fab 4C6
20022 ! part of Fab Jel 103
74133 ! part of retro Diels-Alder catalytic Fab 9D9
71146 ! part of anti-testosterone Fab
59711 ! part of anti-IL2 Fab LNKB-2
20164 ! part of Fv 4155
84861 ! part of Fab specific for Y lipopolysaccharide
99153 ! part of blue fluorescent Fab 19G2
20502 ! part of anti-photoproduct Fab 64M-2
20190 ! part of polysaccharide binding antibody 2H1
20372 ! part of Fab 6B5
20158 ! part of Fab D2.5
19820 ! part of Fab 26-10
20100 ! part of humanized Fab CBR96
20356 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
20358 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
20080 ! part of a polysialic acid-binding Fab
20134 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
19978 ! part of Fab JE142
72993 ! part of scFv 3d5
20487 ! part of blue fluorescent Fab 19G2
84865 ! part of Fab specific for Y lipopolysaccharide
19822 ! part of Fab 26-10
20432 ! part of anti-prion Fab 3F4
20236 ! part of humanized Diels-Alder catalytic Fab
19898 ! part of Fab BV04-01
71142 ! part of anti-testosterone Fab
20041 ! part of scFv diabody L5MK16
85571 ! part of cationic cyclization catalytic Fab 4C6
20028 ! part of Fab R6.5
19814 ! part of Fab B13I2
20292 ! part of Influenza virus hemagglutinin-neutralizing Fab
67003 ! part of scFv 1695; complexed with the epitope peptide from HIV-1 protease
20104 ! part of Fab MBR96
20102 ! part of humanized Fab CBR96
20232 ! part of humanized Diels-Alder catalytic Fab; germline precursor
74141 ! part of retro Diels-Alder catalytic Fab 9D9
19900 ! part of Fab BV04-01
20110 ! part of Fab 1583
65023 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
19800 ! part of Fab DB3
19798 ! part of Fab DB3
20418 ! part of Fab 1696 against HIV-1 protease
19804 ! part of Fab DB3
19802 ! part of Fab DB3
19816 ! part of Fab B13I2
84851 ! part of Fab specific for Y lipopolysaccharide
77367 ! part of anti-gibberellin A4 Fab 4-B8(8)/E9; conflict: annotated in PDB as human protein
91759 ! part of Fab 83.1 against HIV-1 gp120 
20150 ! part of Fab D2.4
20210 ! part of Fab CTM01
20332 ! part of anti-P-glycoprotein Fab MRK-16
19808 ! part of Fab DB3
19806 ! part of Fab DB3
19920 ! part of an anti-sweetener Fab
20030 ! part of neutralizing type 1 poliovirus Fab C3
19906 ! part of Fab 4-4-20
19825 ! VL of antibody 26-10 only
19824 ! VL of antibody 26-10 only !SQ P01642 21-115 #! KV2G_MOUSE IG KAPPA CHAIN V-II REGION 26-10
108172 !MQ P03976 P01837 #! natural chimera !SQ P03976 # KV2E_MOUSE (P03976) Ig kappa chain V-II region 17S29.1
105239 !MQ NA  # artificial chimera
108162 !MQ P03976 P01837 #! natural chimera !SQ P03976 # KV2E_MOUSE (P03976) Ig kappa chain V-II region 17S29.1
105274 !MQ P06310 P01837  !SQ P06310 # KV2F_HUMAN IG KAPPA CHAIN V-II REGION RPMI 6410 PRECURSOR
96305 ! part of Fab s25-2
96301 ! part of Fab s25-2
80623 ! part of anti-HCV Fab 19D9D6
96316 ! part of Fab s25-2
91474 ! part of P-glycoprotein-specific scFv C219; complexed with synthetic epitope peptide, chain P
96310 ! part of Fab s25-2
96324 ! part of Fab s45-18 
19857 ! VL domain only of MCPC603
96296 ! part of Fab s45-18
19780 ! part of Fab 8F5
20366 ! part of anti-HCG Fab 3A2
79123 ! part of anti-HCV Fab 19D9D6
19788 ! part of Fab 17/9
96276 ! part of Fab s25-2
62541 ! part of anti-HIV Fab G3-519
100855 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with a synthetic cyclic peptide
20392 ! part of sterolytic and amidolytic Fv 43c9
96284 ! part of Fab s25-2
20400 ! part of sterolytic and amidolytic Fv 43c9
90424 ! part of anti-anti-idiotypic Fab against human angiotensin II, unliganded form 
20180 ! part of P-glycoprotein-specific scFv C219
19790 ! part of Fab 17/9
20184 ! part of P-glycoprotein-specific scFv C219
19924 ! part of Fab 26/9
76650 ! part of anti-hepatitis B Fab (against PRES1 region)
80116 ! part of anti-HCV Fab 19D9D6; complex with peptide, chain P (related to 1cwx)
100867 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with angiotensin II
19782 ! part of Fab 8F5
19795 ! part of Fab 17/9; chain identifiers are mixed up
20302 ! part of an anti-E-selectin Fab
19858 ! part of Fab MCPC603
19860 ! part of Fab MCPC603
19796 ! part of Fab 17/9
88153 ! part of humanized Fab 8-18c5
90738 ! part of anti-CEA Fv T84.66
20350 ! part of anti-gp120 (HIV-1) Fab 58.2
83425 ! part of anti-angiogenin FAB; conflict: annotated in PDB as human
20172 ! part of Fab F11.2.32 against HIV-1 protease
61923 ! part of humanized Fab GNC92H2
66279 ! part of anti-human Fas Fab HFE7a
20428 ! part of anti-FMDV Fab 4C4
20176 ! part of Fab F11.2.32 against HIV-1 protease
85032 ! part of anti-CEA scFv T84.66; VL to VH linkage: includes linker residues 112-119; assembles as a diabody
20352 ! part of anti-gp120 (HIV-1) Fab 58.2
19874 ! part of Fab 50.1
20354 ! part of anti-gp120 (HIV-1) Fab 58.2
20048 ! part of Fab 40-50
19878 ! part of Fab 50.1
19880 ! part of Fab 50.1
20458 ! part of anti-Pres2 Fab F124
19882 ! part of Fab 59.1
20500 ! part of Fab 13B5 against cytokine receptor common beta chain domain 4
20070 ! part of Fab N10
19884 ! part of Fab 59.1
20438 ! part of the cytochrome P450-arom activity suppressing Fab 32C2
20132 ! part of Fab 25.3 against HIV-1 capsid protein (p24)
20434 ! part of anti-[gonadotropin alpha subunit] Fv
20448 ! part of anti-HIV Fv 0.5B
87349 ! part of anti-VD potassium channel KVAP Fab 33H1
20296 ! part of catalytic Fab 5C8
20298 ! part of catalytic Fab 5C8
20378 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
20300 ! part of catalytic Fab 5C8
83625 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
20074 ! part of Fab 409.5.3
86754 ! part of anti-Pf MSP1 Fab
87344 ! part of anti-VD potassium channel KVAP Fab 6E1
20078 ! part of Fab 409.5.3
19922 ! part of catalytic antibody 1F7 with chorismate mutase activity
72385 ! part of Fab against influenza virus hemagglutinin
20440 ! part of Fab HGR-2 F6, a competitive antagonist of the glucagon receptor
20242 ! part of Fab TP7 against Taq DNA polymerase
20493 ! part of anti-carcinoembryonic scFv MFE-23
20244 ! part of Fab TP7 against Taq DNA polymerase
19988 ! part of Fab 17-Ia
19970 ! part of Fab HyHEL-5
19968 ! part of Fab HyHEL-5
20128 ! part of CD25-binding humanized Fab CHI621
20138 ! part of antibody against the melanoma associated gd2 ganglioside
20294 ! part of Influenza virus hemagglutinin-neutralizing Fab BH151
100456 ! part of anti-trombopoetin Fab tn1
19778 ! part of Fab ANO2
87423 ! part of anti-CLC chloride channel Fab
19972 ! part of Fab HyHEL-5
100474 ! part of anti-trombopoetin Fab tn1
87443 ! part of anti-CLC chloride channel Fab
87433 ! part of anti-CLC chloride channel Fab
19990 ! part of Fv 17-Ia
106115 !MQ P04940 P01837 # natural chimera !SQ P04940 # KV6F_MOUSE IG KAPPA CHAIN V-VI REGION NQ2-17.4.1
20122 ! part of Fab A5B7
20250 ! part of human rhinovirus 14 neutralizing Fab Mab1-IA
20494 ! part of Fab 13B5 against HIV-1 capsid protein p24
19850 ! part of Fab J539
20496 ! part of Fab 13B5 against HIV-1 capsid protein p24
85054 ! part of Fv against Paracoccus denitrificans cytochrome c oxidase
91259 ! part of Fab 29g12
19926 ! part of Fv D1.3
20474 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
99133 ! part of Fv HyHEL-10
19928 ! part of Fv D1.3
94287 ! part of anti-ssDNA Fab
19930 ! part of Fv D1.3
19932 ! part of Fv D1.3
71130 ! part of dsFv MR1; complex with a EGFR-VIII peptide
77061 ! part of Fv HyHEL-10
77058 ! part of Fv HyHEL-10
77064 ! part of Fv HyHEL-10
72317 ! part of anti-hepatitis B Fab pc282
85536 ! part of anti-lysozyme Fab HYHEL-63
20422 ! part of anti-lysozyme Fab HYHEL-63
19934 ! part of Fv D1.3
20360 ! part of anti-cytochrome c Fab E8
80252 ! part of metal chelatase catalytic Fab 7G12; germline antibody; chain identifiers are probably mixed up
19938 ! part of Fv D1.3
19936 ! part of Fv D1.3
20288 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
96928 ! part of Fab against potassium channel KcsA
19940 ! part of Fv D1.3
85576 ! a part of Fab HYHEL-8, L chain is identical to HYHEL-63
19948 ! part of Fv D1.3
19944 ! part of Fv D1.3
85541 ! part of anti-lysozyme Fab HYHEL-63
19946 ! part of Fv D1.3
19942 ! part of Fv D1.3
99130 ! part of Fv HyHEL-10
20106 ! part of Fv E5.2, anti-idiotopic antibody to D1.3 ! CASP1
66648 ! part of Fab 36-71
19950 ! part of Fv D1.3
19954 ! part of Fv D1.3
19952 ! part of Fv D1.3 ! CASP1
93920 ! part of anti-lysozyme Fab F10.6.6
59234 ! part of anti-TGFalpha Fab TAB2
60783 ! part of anti-ampicillin scFv
68128 ! part of Fab against potassium channel KcsA
19956 ! part of Fv D1.3
19958 ! part of Fv D1.3
20116 ! part of Fab 184.1 against OspA
20424 ! part of anti-lysozyme Fab HYHEL-63
20270 ! part of Fab 2E8 specific to the low density lipoprotein receptor binding region of apolipoprotein E
20066 ! part of anti-integrin Fab OPG2
62259 ! part of Fv HyHEL-10
19908 ! part of Fab 36-71
20476 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
66681 ! part of anti-estradiol Fab 57-2
20194 ! part of humanized oxy-cope catalytic Fab az-28
59796 ! part of Fab RU5 inhibiting the collagen binding by the von willebrand factor a3 domain
59242 ! part of anti-TGFalpha Fab TAB2
20068 ! part of anti-integrin Fab OPG2
20082 ! part of humanized Fab 48G7
66082 ! part of anti-ssDNA Fab
20196 ! part of humanized oxy-cope catalytic Fab az-28
20086 ! part of humanized Fab 48G7
20084 ! part of humanized Fab 48G7
20491 ! part of anti-lysozyme scFv 1F9
85581 ! a part of Fab HYHEL-26, L chain is identical to HYHEL-63
71128 ! part of dsFv MR1; complex with a EGFR-VIII peptide
62255 ! part of Fv HyHEL-10
20050 ! part of Fab D44.1
68133 ! part of Fab against potassium channel KcsA
20482 ! part of anti-C60 fullerene Fab
20054 ! part of Fab D44.1
20290 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
72313 ! part of anti-hepatitis B Fab pc287
20410 ! part of catalytic Fab 7C8
66019 ! part of anti-ampicillin scFv
20362 ! part of anti-cytochrome c Fab E8
96926 ! part of Fab against potassium channel KcsA
66717 ! part of anti-estradiol Fab 57-2
20032 ! part of an anti-cyclosporin A Fab
20426 ! part of anti-lysozyme Fab HYHEL-63
20376 ! part of metal chelatase catalytic Fab 7G12; mature antibody
20286 ! part of catalytic antibody 29G11 with esterase activity
96938 ! part of Fab against potassium channel KcsA
20364 ! part of anti-cytochrome c Fab E8
62252 ! part of Fv HyHEL-10
97511 ! part of Fab 14F7
19960 ! part of Fab D1.3
59555 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
19980 ! part of Fab NC41
60791 ! part of anti-ampicillin scFv
20402 ! part of humanized Fab R24 from murine ascites
20328 ! part of humanized Fab-12 neutralizing VEGF; affinity matured
19962 ! part of Fab D1.3
19974 ! part of Fv HyHEL-10
19964 ! part of D1.3 anti-idiotope Fab E225
20060 ! part of Fab NC10; only Fv coordinates are included
72094 ! part of anti-human tissue factor Fab D3
20088 ! part of humanized Fab 48G7
20014 ! part of Fab 17E8
60787 ! part of anti-ampicillin scFv
19982 ! part of Fab NC41
20059 ! part of Fab NC10; only Fv coordinates are included
19966 ! part of Fv D11.15
20062 ! part of Fab NC10; only Fv coordinates are included
20380 ! part of antibody directed against the musk odorant traseolide
72296 ! part of anti-hepatitis B Fab pc287; complex with ps1 peptide
20216 ! part of anti-human tissue factor Fab 5G9
72309 ! part of anti-hepatitis B Fab pc282; complex with ps1 peptide
20046 ! part of Fab MoPC21
19986 ! part of Fab NC41
20206 ! part of Fv against Paracoccus denitrificans cytochrome c oxidase
19984 ! part of Fab NC41
19886 ! part of Fab Yst9.1
19844 ! part of Fab R19.9
19842 ! part of Fab R19.9
20200 ! part of humanized oxy-cope catalytic Fab az-28
19766 ! part of intact IgG2a antibody Mab231
20464 ! part of Fab MAK33; conflict: annotated in PDB as human protein
20120 ! part of Fab LA-2 against OspA
100119 ! part of catalytic Fab 14d9
20108 ! part of Fab GH1002
72305 ! part of anti-hepatitis B Fab pc283; complexed with ps1 peptide
20228 ! part of Fab Desire-1
100111 ! part of catalytic Fab 14d9
96933 ! part of Fab against potassium channel KcsA
19784 ! part of humanized Fab B72.3
77326 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
20026 ! part of Fab F9.13.7
66958 ! part of anti-estradiol Fab 17E12E5
20324 ! part of humanized Fab-12 neutralizing VEGF
20064 ! part of Fab NC10; only Fv coordinates are included
20204 ! part of humanized oxy-cope catalytic Fab az-28
20072 ! part of Fab 730.1.4
20222 ! part of Fab A6
20334 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20336 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20338 ! part of anti-gp120 (HIV-1) Fab CB 4-1
66962 ! part of anti-estradiol Fab 17E12E5
20340 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20208 ! part of Fv against Paracoccus denitrificans cytochrome c oxidase
20344 ! part of anti-gp120 (HIV-1) Fab CB 4-1
94688 ! part of Fab 6A6
20342 ! part of anti-gp120 (HIV-1) Fab CB 4-1
19770 ! part of intact IgG1 antibody Mab61.1.3
20012 ! part of Fab CNJ206
20220 ! part of anti-human tissue factor Fab 5G9
20346 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20472 ! part of anti-bet v1 Fab BV16
20348 ! part of anti-gp120 (HIV-1) Fab CB 4-1
87865 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
20274 ! part of Fab 28 against HIV-1 RT
99058 ! part of Fab 28 against HIV-1 RT
80062 ! part of Fab 28 against HIV-1 RT
73278 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
19976 ! part of Fab HyHEL-10
61420 ! part of Fab 28 against HIV-1 RT
80209 ! part of Fab 28 against HIV-1 RT
20436 ! part of anti-[gonadotropin beta subunit] Fv
20406 ! part of Fab R24 from murine ascites
71573 ! part of Fab 28 against HIV-1 RT
80500 ! part of metal chelatase catalytic Fab 7G12; chimeric germline antibody
85708 ! part of metal chelatase catalytic Fab 7G12; chimeric germline antibody
80496 ! part of metal chelatase catalytic Fab 7G12; chimeric mature antibody
20006 ! part of Fab CNJ206; H-chains in this entry seem to be mistraced in VH region
20308 ! part of a chimeric anti-gamma-interferon Fab
80494 ! part of metal chelatase catalytic Fab 7G12; chimeric affinity matured antibody !SQ P01642 21-115 #! KV5I_MOUSE Ig kappa chain V-V region L7 precursor
104681 !SQ NA # part of Fab 28 against HIV-1 RT 
73958 ! part of anti-IL-10 Fab 9D7
20318 ! part of humanized therapeutic antibody CAMPATH-1H
20316 ! part of therapeutic monoclonal antibody CAMPATH-1G
20414 ! part of antibody against the main immunogenic region of the human muscle acetylcholine receptor
59888 ! part of Fab 198 against acetylcholine receptor
20320 ! part of antibody to CAMPATH-1H humanized Fab
20417 ! part of scFv MAB198 against the main immunogenic region of the human muscle acetylcholine receptor; order: VH-linker-VL
19856 ! VL domain only of humanized antibody MCPC603
73658 ! part of humanized anti-ERBb2 Fab 2C4
67053 ! part of humanized Fab D3H44 against human tissue factor
19852 ! part of humanized Fv H52
67047 ! part of humanized Fab D3H44 against human tissue factor
87212 ! part of engineered Fab 2G12
88508 ! part of humanized HIV-1 neutralizing Fab 2F5
20517 ! VL domain of synthetic antibody M29B; "reversed" dimerisation mode
88504 ! part of humanized HIV-1 neutralizing Fab 2F5
19864 ! part of humanized Fv 4D5, herceptin
87065 ! part of engineered Fab 2G12
19868 ! part of humanized Fab 4D5, herceptin
20126 ! part of humanized Fab A5B7
107483 !SQ NA # engineered antibody
19872 ! part of humanized Fab 4D5, herceptin
80318 ! part of humanized Fab 4D5, herceptin
84972 ! part of humanized anti-alpha1 integrin I-domain Fab; only V domain is ordered
84969 ! part of humanized anti-alpha1 integrin I-domain Fab
20214 ! part of humanized Fab CTM01
19854 ! part of humanized Fab H52
20306 ! part of a humanized anti-gamma-interferon Fab
20280 ! part of humanized anti-lysozyme Fv HuLys11
107487 !SQ NA # engineered antibody
76785 ! part of humanized anti-human Fas Fab HFE7A
20285 ! part of humanized anti-lysozyme Fv HuLys11
94680 ! part of humanized Fab D3H44 against human tissue factor
71161 ! part of humanized Fab 5C8 against C40 ligand
98628 ! part of anti-ERBb2 Fab Pertuzumab
87220 ! part of engineered Fab 2G12
105237 !MQ NA P01857 # artificial chimera !SQ NA # humanized antibody
107888 !MQ NA P01834 # artificial chimera !SQ NA # Humanized antibody
88534 ! VL-lambda domains of human antibodies are clustered by the sequence similarity within the germline encoded segment and then by the size of the complementarity determining regions CDR1 and CDR2, so the clusters may correspond to putative germline families in the human genome; mouse VL-lambda domains belong to a single germline family
104136 !SQ P06317 # Ig lambda chain V-VI region SUT
20560 ! VL dimer of Bence-Jones protein JTO
104336 !SQ NA # Bence-Jones protein JTO
20562 ! VL dimer of Bence-Jones protein WIL
20523 ! VL of Bence-Jones protein RHE
98152 ! part of anti HIV-1 gp120-reactive Fab E51
19846 ! part of Fab KOL
91947 ! part of Fab 10c12 against factor IX Gla domain 
20525 ! VL dimer of Bence-Jones protein LOC
20527 ! VL dimer of Bence-Jones protein LOC
20529 ! VL dimer of Bence-Jones protein LOC
95587 ! part of anti HIV-1 Fab 447-52d
19848 ! part of antibody KOL; intact protein but only Fab's can be seen in the crystal structure
20192 ! part of Fab B7-15A2
19776 ! part of Fab NEW
84610 ! part of amyloidogenic protein BUR
71899 ! part of amyloidogenic protein BUR
84614 ! part of amyloidogenic protein BUR
20566 ! part of the antibody MCG light chain dimer
20568 ! part of the antibody MCG light chain dimer
20570 ! part of the antibody MCG light chain dimer
20574 ! part of the antibody MCG light chain dimer
20572 ! part of the antibody MCG light chain dimer
20576 ! part of the antibody MCG light chain dimer
20578 ! part of the antibody MCG light chain dimer
20580 ! part of the antibody MCG light chain dimer
20582 ! part of the antibody MCG light chain dimer
20584 ! part of the antibody MCG light chain dimer
20588 ! part of the antibody MCG light chain dimer
20586 ! part of the antibody MCG light chain dimer
20590 ! part of the antibody MCG light chain dimer
20592 ! part of the antibody MCG light chain dimer
20596 ! part of the antibody MCG light chain dimer
20594 ! part of the antibody MCG light chain dimer
20598 ! part of the antibody MCG light chain dimer
20600 ! part of the antibody MCG light chain dimer
20602 ! part of heterologous L chain dimer MCG-WEIR
20563 ! part of intact antibody MCG
19774 ! part of Fab HIL
20558 ! part of Bence-Jones protein CLE
20272 ! part of IgM rheumatoid factor Fab
19888 ! part of Fv SE155-4
95519 ! part of anti-morphine Fab 9b1
20252 ! part of Fv B1-8
95523 ! part of anti-morphine Fab 9b1
20254 ! part of Fv B1-8
19892 ! part of Fab SE155-4
19890 ! part of Fab SE155-4
19894 ! part of Fab SE155-4
19896 ! part of Fab SE155-4
20368 ! part of tumor-specific Fab SM3 against epithelial mucin Muc1
91785 ! part of Fab 2d12.5
91793 ! part of Fab 2d12.5
20450 ! part of anti-carbohydrate Fab S-20-4
19838 ! part of Fab Cha255
20260 ! part of Fv B1-8
20452 ! part of anti-carbohydrate Fab S-20-4
19910 ! part of Fab HC19
94099 ! part of anti-GCN4 peptide scFv
20090 ! part of Fab N1G9
91903 ! part of cocaine hydrolytic Fab 15a10
20092 ! part of Fab N1G9
19840 ! part of Fab Cha255
94105 ! part of anti-GCN4 peptide scFv
66951 ! part of anti-estradiol Fab 10G6D6
20498 ! part of Fv M3C65; conflict: annotated in PDB as human protein
66923 ! part of anti-estradiol Fab 10G6D6
19914 ! part of Fab HC19
19916 ! part of Fab HC19
20454 ! part of anti-carbohydrate Fab S-20-4
20480 ! part of anti-sweetener Fab NC10.14
20098 ! part of an anti-nitrophenol Fab
94686 ! part of Fab 6A6
19912 ! part of Fab HC19
92708 ! part of IgE Fv spe-7
92724 ! part of IgE Fv spe-7
92716 ! part of IgE Fv spe-7
92780 ! part of IgE Fv spe-7
92732 ! part of IgE Fv spe-7
92740 ! part of IgE Fv spe-7
92746 ! part of IgE Fv spe-7
20188 ! part of Fab H57
88543 ! VH domains of human and mouse antibodies are clustered by the sequence similarity within the germline encoded segment and then by the size of the complementarity determining regions CDR1 and CDR2, so the clusters may correspond to putative germline families in the species genomes; VH domains with artificial or grafted exogenous CDRs are listed as engineered species
98150 ! part of anti HIV-1 gp120-reactive Fab E51
91530 ! part of an anti HIV-1 Fab
98133 ! part of anti HIV-1 gp120-reactive Fab 48D
98158 ! part of anti HIV-1 gp120-reactive Fab 412D
62646 ! part of intact IgG B12 antibody
20095 ! part of humanized Fab TR1.9
97479 ! part of HIV-1 neutralizing Fab x5
67345 ! part of an anti-blood group A Fv
98143 ! part of anti HIV-1 gp120-reactive Fab 17B
20263 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
98201 ! part of anti HIV-1 gp120-reactive Fab 17B
20265 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
61441 ! part of intact IgG B12 antibody
98208 ! part of anti HIV-1 gp120-reactive Fab 17B
20267 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
98196 ! part of anti HIV-1 gp120-reactive Fab 47E
19777 ! part of Fab NEW
19833 ! part of Fab Kau cold agglutinin IgM
19837 ! part of Fab Kau cold agglutinin IgM
20564 ! part of intact antibody MCG
19775 ! part of Fab HIL
19847 ! part of Fab KOL
20193 ! part of Fab B7-15A2
91945 ! part of Fab 10c12 against factor IX Gla domain 
19829 ! part of IgM Fv MEZ
19827 ! part of IgM Fv POT
19811 ! part of Fab 3D6
20447 ! part of IgM RF 2A2
60989 ! part of IgM RF 2A2
20273 ! part of IgM rheumatoid factor Fab
19849 ! part of antibody KOL; intact protein but only Fab's can be seen in the crystal structure
95583 ! part of anti HIV-1 Fab 447-52d
20383 ! part of anti-dansyl Fv
96307 ! part of Fab s25-2 
96303 ! part of Fab s25-2 
20385 ! part of anti-dansyl Fv
96318 ! part of Fab s25-2 
96589 ! part of anti-cocaine Fab M82G2
96014 ! part of anti-cocaine Fab M82G2
96312 ! part of Fab s25-2 
96326 ! part of Fab s45-18 
95403 ! part of Fab Sya/J6
96298 ! part of Fab s45-18 
97518 ! part of anti-cocaine Fab M82G2
20113 ! part of Fab 28B4
20367 ! part of anti-HCG Fab 3A2
97372 ! part of anti-cocaine Fab M82G2
19905 ! part of Fab 4-4-20
97522 ! part of anti-cocaine Fab M82G2
96278 ! part of Fab s25-2 
20369 ! part of tumor-specific Fab SM3 against epithelial mucin Muc1
20115 ! part of Fab 28B4
100853 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with a synthetic cyclic peptide
20123 ! part of Fab A5B7
65017 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
20305 ! part of catalytic Fab 33F12 with an aldolase activity
96286 ! part of Fab s25-2 
84863 ! part of Fab specific for Y lipopolysaccharide
90422 ! part of anti-anti-idiotypic Fab against human angiotensin II, unliganded form 
84867 ! part of Fab specific for Y lipopolysaccharide
19899 ! part of Fab BV04-01
19887 ! part of Fab Yst9.1
100452 ! part of anti-trombopoetin Fab tn1
65025 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
19901 ! part of Fab BV04-01
100865 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with angiotensin II 
84853 ! part of Fab specific for Y lipopolysaccharide
19859 ! part of Fab MCPC603
20075 ! part of Fab 409.5.3
19861 ! part of Fab MCPC603
19907 ! part of Fab 4-4-20
100466 ! part of anti-trombopoetin Fab tn1
20079 ! part of Fab 409.5.3 !SQ P01796 #! HV27_MOUSE Ig heavy chain V-III region A4
66688 ! part of catalytic Fab 1D4
66692 ! part of catalytic Fab 1D4
20167 ! part of hydrolytic antibody 6D9
74123 ! part of retro Diels-Alder catalytic Fab 9D9
74115 ! part of retro Diels-Alder catalytic Fab 9D9
20169 ! part of hydrolytic antibody 6D9
77799 ! part of anti-testosterone Fab 77
99143 ! part of blue fluorescent Fab 19G2
77795 ! part of anti-testosterone Fab 77
74131 ! part of retro Diels-Alder catalytic Fab 9D9
71144 ! part of anti-testosterone Fab
99151 ! part of blue fluorescent Fab 19G2
20486 ! part of blue fluorescent Fab 19G2
71140 ! part of anti-testosterone Fab
74139 ! part of retro Diels-Alder catalytic Fab 9D9
77363 ! part of anti-gibberellin A4 Fab 4-B8(8)/E9; conflict: annotated in PDB as human protein
85053 ! part of Fv against Paracoccus denitrificans cytochrome c oxidase
71131 ! part of dsFv MR1; complex with a EGFR-VIII peptide
20137 ! part of Fab MN14C11.6
20067 ! part of anti-integrin Fab OPG2
19789 ! part of Fab 17/9
19851 ! part of Fab J539
20161 ! part of Fv 4155
83427 ! part of anti-angiogenin FAB; conflict: annotated in PDB as human
20069 ! part of anti-integrin Fab OPG2
20247 ! part of anticancer Fv B1; disulfide-stabilized
20163 ! part of Fv 4155
71129 ! part of dsFv MR1; complex with a EGFR-VIII peptide
20173 ! part of Fab F11.2.32 against HIV-1 protease
20451 ! part of anti-carbohydrate Fab S-20-4
20033 ! part of an anti-cyclosporin A Fab
19839 ! part of Fab Cha255
20165 ! part of Fv 4155
20453 ! part of anti-carbohydrate Fab S-20-4
20403 ! part of humanized Fab R24 from murine ascites
20191 ! part of polysaccharide binding antibody 2H1
20429 ! part of anti-FMDV Fab 4C4
20101 ! part of humanized Fab CBR96
20177 ! part of Fab F11.2.32 against HIV-1 protease
19791 ! part of Fab 17/9
19925 ! part of Fab 26/9
20207 ! part of Fv against Paracoccus denitrificans cytochrome c oxidase
20047 ! part of Fab MoPC21
19815 ! part of Fab B13I2
20105 ! part of Fab MBR96
20103 ! part of humanized Fab CBR96
19841 ! part of Fab Cha255
19767 ! part of intact IgG2a antibody Mab231
20465 ! part of Fab MAK33; conflict: annotated in PDB as human protein
76648 ! part of anti-hepatitis B Fab (against PRES1 region)
87421 ! part of anti-CLC chloride channel Fab
19794 ! part of Fab 17/9; chain identifiers are mixed up
19817 ! part of Fab B13I2
20333 ! part of anti-P-glycoprotein Fab MRK-16
20209 ! part of Fv against Paracoccus denitrificans cytochrome c oxidase
20455 ! part of anti-carbohydrate Fab S-20-4
19797 ! part of Fab 17/9
20013 ! part of Fab CNJ206
20437 ! part of anti-[gonadotropin beta subunit] Fv
20407 ! part of humanized Fab R24 from murine ascites
87441 ! part of anti-CLC chloride channel Fab
87431 ! part of anti-CLC chloride channel Fab
108170 !MQ P01811 P22436 #! natural chimera !SQ P01811 # HV41_MOUSE (P01811) Ig heavy chain V region UPC10
108164 !MQ P01811 P22436 #! natural chimera !SQ P01811 # HV41_MOUSE (P01811) Ig heavy chain V region UPC10
20007 ! part of Fab CNJ206; H-chains in this entry seem to be mistraced in VH region
20361 ! part of anti-cytochrome c Fab E8
19781 ! part of Fab 8F5
20107 ! part of Fv E5.2, anti-idiotopic antibody to D1.3 ! CASP1
20431 ! part of anti-prion Fab 3F4
20271 ! part of Fab 2E8 specific to the low density lipoprotein receptor binding region of apolipoprotein E
20297 ! part of catalytic Fab 5C8
62539 ! part of anti-HIV Fab G3-519
20083 ! part of humanized Fab 48G7
20085 ! part of humanized Fab 48G7
20087 ! part of humanized Fab 48G7
20490 ! part of anti-lysozyme scFv 1F9
20299 ! part of catalytic Fab 5C8
20363 ! part of anti-cytochrome c Fab E8
20492 ! part of anti-carcinoembryonic scFv MFE-23
20365 ! part of anti-cytochrome c Fab E8
20089 ! part of humanized Fab 48G7
20301 ! part of catalytic Fab 5C8
72092 ! part of anti-human tissue factor Fab D3
20217 ! part of anti-human tissue factor Fab 5G9
20433 ! part of anti-prion Fab 3F4
20181 ! part of P-glycoprotein-specific scFv C219
20185 ! part of P-glycoprotein-specific scFv C219
85033 ! part of anti-CEA scFv T84.66; VL to VH linkage: linker residues 112-119; assembles as a diabody
19783 ! part of Fab 8F5
20303 ! part of an anti-E-selectin Fab
66956 ! part of anti-estradiol Fab 17E12E5
66960 ! part of anti-estradiol Fab 17E12E5
20221 ! part of anti-human tissue factor Fab 5G9
91302 ! part of the esterolytic Fab ms6-164
91257 ! part of Fab 29g12
97879 ! part of Diels-Alder catalytic Fab 13G5
90737 ! part of anti-CEA Fv T84.66
20475 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
91290 ! part of the esterolytic Fab ms6-164
19889 ! part of Fv SE155-4
95517 ! part of anti-morfine Fab 9b1
20253 ! part of Fv B1-8; this domain is identical to the N-terminal domain of scFv 1NQB
91475 ! part of P-glycoprotein-specific scFv C219; complexed with synthetic epitope peptide, chain P
94289 ! part of anti-ssDNA Fab
20463 ! part of catalytic Fab 4B2
20495 ! part of Fab 13B5 against HIV-1 capsid protein p24
80254 ! part of metal chelatase catalytic Fab 7G12; germline antibody; chain identifiers are probably mixed up
97875 ! part of Diels-Alder catalytic Fab 13G5
96930 ! part of Fab against potassium channel KcsA
20044 ! part of scFv trivalent antibody; N-terminal, VH domain is from B1-8 antibody (1A6U CH H); C-terminal, VL domain is from NQ11 antibody
91298 ! part of the esterolytic Fab ms6-164
95521 ! part of anti-morfine Fab 9b1
66646 ! part of Fab 36-71
20241 ! part of Diels-Alder catalytic Fab 13G5
20255 ! part of Fv B1-8; this domain is identical to the N-terminal domain of scFv 1NQB
20141 ! part of Fab D2.3
20143 ! part of Fab D2.3
93922 ! part of anti-lysozyme Fab F10.6.6
91281 ! part of the esterolytic Fab ms6-164
72765 ! part of Fab D2.3
72760 ! part of Fab D2.3
68126 ! part of Fab against potassium channel KcsA
19891 ! part of Fab SE155-4
59232 ! part of anti-TGFalpha Fab TAB2
19895 ! part of Fab SE155-4
19893 ! part of Fab SE155-4
20145 ! part of Fab D2.3
60784 ! part of anti-ampicillin scFv
20155 ! part of Fab D2.5
20153 ! part of Fab D2.5
20477 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
19909 ! part of Fab 36-71
19897 ! part of Fab SE155-4
59238 ! part of anti-TGFalpha Fab TAB2
20195 ! part of humanized oxy-cope catalytic Fab az-28
20197 ! part of humanized oxy-cope catalytic Fab az-28
66084 ! part of anti-ssDNA Fab
20147 ! part of Fab D2.3
91270 ! part of the esterolytic Fab ms6-164
20051 ! part of Fab D44.1
91286 ! part of the esterolytic Fab ms6-164
20483 ! part of anti-C60 fullerene Fab
20157 ! part of Fab D2.5
20019 ! part of Fab Jel 103
20055 ! part of Fab D44.1
68131 ! part of Fab against potassium channel KcsA
66018 ! part of anti-ampicillin scFv
20017 ! part of Fab Jel 103
20021 ! part of Fab Jel 103
19919 ! part of an anti-sweetener Fab
77345 ! part of anti-photoproduct Fab 64M-2
96924 ! part of Fab against potassium channel KcsA
20377 ! part of metal chelatase catalytic Fab 7G12; mature antibody
20287 ! part of catalytic antibody 29G11 with esterase activity
20023 ! part of Fab Jel 103
96940 ! part of Fab against potassium channel KcsA
20261 ! part of Fv B1-8; this domain is identical to the N-terminal domain of scFv 1NQB
66277 ! part of anti-human Fas Fab hfe7a
97509 ! part of Fab 14F7
20373 ! part of Fab 6B5
20159 ! part of Fab D2.5
20503 ! part of anti-photoproduct Fab 64M-2
60792 ! part of anti-ampicillin scFv
19965 ! part of D1.3 anti-idiotope Fab E225
20091 ! part of Fab N1G9
20251 ! part of human rhinovirus 14 neutralizing Fab Mab1-IA
20357 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
19821 ! part of Fab 26-10
20061 ! part of Fab NC10; only Fv coordinates are included
72992 ! part of scFv 3d5
20081 ! part of a polysialic acid-binding Fab
20359 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
20135 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
19979 ! part of Fab JE142
20015 ! part of Fab 17E8
91901 ! part of cocaine hydrolytic Fab 15a10
60788 ! part of anti-ampicillin scFv
20093 ! part of Fab N1G9
19823 ! part of Fab 26-10
19989 ! part of Fab 17-Ia
19967 ! part of Fv D11.15
20063 ! part of Fab NC10; only Fv coordinates are included
20058 ! part of Fab NC10; only Fv coordinates are included
20129 ! part of CD25-binding humanized Fab CHI621
19969 ! part of Fab HyHEL-5
20040 ! part of scFv diabody L5MK16
19971 ! part of Fab HyHEL-5
20029 ! part of Fab R6.5
19843 ! part of Fab R19.9
20295 ! part of Influenza virus hemagglutinin-neutralizing Fab BH151
19845 ! part of Fab R19.9
20139 ! part of antibody against the melanoma associated gd2 ganglioside
20293 ! part of Influenza virus hemagglutinin-neutralizing Fab
20201 ! part of humanized oxy-cope catalytic Fab az-28
20497 ! part of Fab 13B5 against HIV-1 capsid protein p24
100121 ! part of catalytic Fab 14d9
66953 ! part of anti-estradiol Fab 10G6D6
20229 ! part of Fab Desire-1
20459 ! part of anti-Pres2 Fab F124
100113 ! part of catalytic Fab 14d9
96935 ! part of Fab against potassium channel KcsA
19785 ! part of humanized Fab B72.3
66925 ! part of anti-estradiol Fab 10G6D6
19973 ! part of Fab HyHEL-5
20027 ! part of Fab F9.13.7
20501 ! part of Fab 13B5 against cytokine receptor common beta chain domain 4
20151 ! part of Fab D2.4
20335 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20065 ! part of Fab NC10; only Fv coordinates are included
20211 ! part of Fab CTM01
20205 ! part of humanized oxy-cope catalytic Fab az-28
20339 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20341 ! part of anti-gp120 (HIV-1) Fab CB 4-1
19921 ! part of an anti-sweetener Fab
20337 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20099 ! part of an anti-nitrophenol Fab
20345 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20347 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20343 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20031 ! part of neutralizing type 1 poliovirus Fab C3
19771 ! part of intact IgG1 antibody Mab61.1.3
88155 ! part of humanized Fab 8-18c5
20473 ! part of anti-bet v1 Fab BV16
20349 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20133 ! part of Fab 25.3 against HIV-1 capsid protein (p24)
19923 ! part of catalytic antibody 1F7 with chorismate mutase activity
20435 ! part of anti-[gonadotropin alpha subunit] Fv
20449 ! part of anti-HIV Fv 0.5B
19991 ! part of Fv 17-Ia
80502 ! part of metal chelatase catalytic Fab 7G12; chimeric germline antibody
85706 ! part of metal chelatase catalytic Fab 7G12; chimeric germline antibody
80498 ! part of metal chelatase catalytic Fab 7G12; chimeric mature antibody
20309 ! part of a chimeric anti-gamma-interferon Fab
80492 ! part of metal chelatase catalytic Fab 7G12; chimeric affinity matured antibody !SQ P01750 20-116 #! HV06_MOUSE Ig heavy chain V region 102 precursor
106113 !MQ P01750 P01863 # natural chimera !SQ P01750 # HV06_MOUSE Ig heavy chain V region 102 precursor
20411 ! part of catalytic Fab 7C8
80621 ! part of anti-HCV Fab 19D9D6
85325 ! part of scFv 1695
79125 ! part of anti-HCV Fab 19D9D6
66679 ! part of anti-estradiol Fab 57-2
19903 ! part of Fab TE33
20239 ! part of Diels-Alder catalytic Fab 1E9
66715 ! part of anti-estradiol Fab 57-2
61925 ! part of humanized Fab GNC92H2
19981 ! part of Fab NC41
20329 ! part of humanized Fab-12 neutralizing VEGF; affinity matured
19983 ! part of Fab NC41
20237 ! part of humanized Diels-Alder catalytic Fab
19985 ! part of Fab NC41
19987 ! part of Fab NC41
67004 ! part of scFv 1695; complexed with the epitope peptide from HIV-1 protease
20233 ! part of humanized Diels-Alder catalytic Fab
20121 ! part of Fab LA-2 against OspA
20109 ! part of Fab GH1002
19799 ! part of Fab DB3
19801 ! part of Fab DB3
80114 ! part of anti-HCV Fab 19D9D6; complex with peptide, chain P (related to 1cwx)
20419 ! part of Fab 1696 against HIV-1 protease
19805 ! part of Fab DB3
19803 ! part of Fab DB3
20325 ! part of humanized Fab-12 neutralizing VEGF
20073 ! part of Fab 730.1.4
19807 ! part of Fab DB3
19809 ! part of Fab DB3
86756 ! part of anti-Pf MSP1 Fab
107215 !MQ P01631 P01837 #! natural chimera !SQ P01631 # KV2G_MOUSE (P01631) Ig kappa chain V-II region 26-10
107192 !MQ P01631 P01837 #! natural chimera !SQ P01631 # KV2G_MOUSE (P01631) Ig kappa chain V-II region 26-10
107213 !MQ P06327 P01864 #! natural chimera !SQ P06327 20-117 # HV52_MOUSE (P06327) Ig heavy chain V region VH558 A1/A4 precursor; 57% sequence identity
107190 !MQ P06327 P01864 #! natural chimera !SQ P06327 20-117 # HV52_MOUSE (P06327) Ig heavy chain V region VH558 A1/A4 precursor; 57% sequence identity
107220 !MQ P01631 P01837 #! natural chimera !SQ P01631 # KV2G_MOUSE (P01631) Ig kappa chain V-II region 26-10
107218 !MQ P06327 P01864 #! natural chimera !SQ P06327 20-117 # HV52_MOUSE (P06327) Ig heavy chain V region VH558 A1/A4 precursor; 57% sequence identity
19927 ! part of Fv D1.3
19929 ! part of Fv D1.3
19933 ! part of Fv D1.3
19931 ! part of Fv D1.3
19935 ! part of Fv D1.3
19937 ! part of Fv D1.3
19939 ! part of Fv D1.3
20289 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
19941 ! part of Fv D1.3
19945 ! part of Fv D1.3
19943 ! part of Fv D1.3
19949 ! part of Fv D1.3
19947 ! part of Fv D1.3
19955 ! part of Fv D1.3
19951 ! part of Fv D1.3
19953 ! part of Fv D1.3 ! CASP1
19959 ! part of Fv D1.3
19957 ! part of Fv D1.3
59790 ! part of Fab RU5 inhibiting the collagen binding by the von willebrand factor a3 domain
91787 ! part of Fab 2d12.5
91795 ! part of Fab 2d12.5
20291 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
20393 ! part of sterolytic and amidolytic Fv 43c9
20401 ! part of sterolytic and amidolytic Fv 43c9
19911 ! part of Fab HC19
94098 ! part of anti-GCN4 peptide scFv
19961 ! part of Fab D1.3
19963 ! part of Fab D1.3
20049 ! part of Fab 40-50
20111 ! part of Fab 1583
94104 ! part of anti-GCN4 peptide scFv
20499 ! part of Fv M3C65; conflict: annotated in PDB as human protein
19915 ! part of Fab HC19
19917 ! part of Fab HC19
19913 ! part of Fab HC19
19875 ! part of Fab 50.1
19881 ! part of Fab 50.1
19879 ! part of Fab 50.1
20223 ! part of Fab A6
104679 !SQ NA # part of Fab 28 against HIV-1 RT 
20481 ! part of anti-sweetener Fab NC10.14
20275 ! part of Fab 28 against HIV-1 RT
99056 ! part of Fab 28 against HIV-1 RT
80060 ! part of Fab 28 against HIV-1 RT
61422 ! part of Fab 28 against HIV-1 RT
80207 ! part of Fab 28 against HIV-1 RT
71571 ! part of Fab 28 against HIV-1 RT
85555 ! part of cationic cyclization catalytic Fab 4C6
97859 ! part of cationic cyclization catalytic Fab 4C6
97871 ! part of cationic cyclization catalytic Fab 4C6
97867 ! part of cationic cyclization catalytic Fab 4C6
97855 ! part of cationic cyclization catalytic Fab 4C6
72315 ! part of anti-hepatitis B Fab pc282
97863 ! part of cationic cyclization catalytic Fab 4C6
20351 ! part of anti-gp120 (HIV-1) Fab 58.2
87351 ! part of anti-VD potassium channel KVAP Fab 33H1
59705 ! part of anti-IL2 Fab LNKB-2
20243 ! part of Fab TP7 against Taq DNA polymerase
72311 ! part of anti-hepatitis B Fab pc287
97851 ! part of cationic cyclization catalytic Fab 4C6
59709 ! part of anti-IL2 Fab LNKB-2
20245 ! part of Fab TP7 against Taq DNA polymerase
59554 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
20379 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
72294 ! part of anti-hepatitis B Fab pc287; complex with ps1 peptide
20381 ! part of antibody directed against the musk odorant traseolide
72307 ! part of anti-hepatitis B Fab pc282; complex with ps1 peptide
85573 ! part of cationic cyclization catalytic Fab 4C6
20353 ! part of anti-gp120 (HIV-1) Fab 58.2
20355 ! part of anti-gp120 (HIV-1) Fab 58.2
19779 ! part of Fab ANO2
83627 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
72303 ! part of anti-hepatitis B Fab pc283; complex with ps1 peptide
77325 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
20071 ! part of Fab N10
20439 ! part of the cytochrome P450-arom activity suppressing Fab 32C2
87864 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
87346 ! part of anti-VD potassium channel KVAP Fab 6E1
73277 ! part of Fv against Rieske protein from the yeast cytochrome bc1 complex
72383 ! part of Fab against influenza virus hemagglutinin
105272 !MQ P18532 P01868 # natural 'chimera' !SQ P18532 # HV61_MOUSE Ig heavy chain V region 1B43 precursor
99132 ! part of Fv HyHEL-10
77063 ! part of Fv HyHEL-10
77060 ! part of Fv HyHEL-10
77057 ! part of Fv HyHEL-10
85538 ! part of anti-lysozyme Fab HYHEL-63
20423 ! part of anti-lysozyme Fab HYHEL-63
85578 ! a part of Fab HYHEL-8
85543 ! part of anti-lysozyme Fab HYHEL-63
99129 ! part of Fv HyHEL-10
62258 ! part of Fv HyHEL-10
20117 ! part of Fab 184.1 against OspA
20425 ! part of anti-lysozyme Fab HYHEL-63
85583 ! a part of Fab HYHEL-26
20441 ! part of Fab HGR-2 F6, a competitive antagonist of the glucagon receptor
62254 ! part of Fv HyHEL-10
20427 ! part of anti-lysozyme Fab HYHEL-63
62251 ! part of Fv HyHEL-10
19975 ! part of Fv HyHEL-10
91755 ! part of Fab 83.1 against HIV-1 gp120 
19977 ! part of Fab HyHEL-10
19883 ! part of Fab 59.1
19885 ! part of Fab 59.1
92707 ! part of IgE Fv spe-7
73954 ! part of anti-IL-10 Fab 9D7
92720 ! part of IgE Fv spe-7
20319 ! part of humanized therapeutic antibody CAMPATH-1H
92712 ! part of IgE Fv spe-7
92779 ! part of IgE Fv spe-7
20317 ! part of therapeutic monoclonal antibody CAMPATH-1G
20415 ! part of antibody against the main immunogenic region of the human muscle acetylcholine receptor
92728 ! part of IgE Fv spe-7
92736 ! part of IgE Fv spe-7
59890 ! part of Fab 198 against acetylcholine receptor
20321 ! part of antibody to CAMPATH-1H humanized Fab
20416 ! part of scFv MAB198 against the main immunogenic region of the human muscle acetylcholine receptor; order: VH-linker-VL
92744 ! part of IgE Fv spe-7
20189 ! part of Fab H57
93297 ! camelized human VH
73656 ! part of humanized anti-ERBb2 Fab 2C4
67051 ! part of humanized Fab D3H44 against human tissue factor
19853 ! part of humanized Fv H52
67045 ! part of humanized Fab D3H44 against human tissue factor
87214 ! part of engineered Fab 2G12
93028 ! soluble VH Hel4, resistant to aggregation
88506 ! part of humanized HIV-1 neutralizing Fab 2F5
20227 ! part of Fab M41 (artificial design)
88502 ! part of humanized HIV-1 neutralizing Fab 2F5
19865 ! part of humanized Fv 4D5, herceptin
87061 ! part of engineered Fab 2G12
19869 ! part of humanized Fab 4D5, herceptin
20127 ! part of humanized Fab A5B7
107481 !SQ NA # engineered antibody
19873 ! part of humanized Fab 4D5, herceptin
80320 ! part of humanized Fab 4D5, herceptin
84967 ! part of humanized anti-alpha1 integrin I-domain Fab
84971 ! part of humanized anti-alpha1 integrin I-domain Fab; only V domain is ordered
19855 ! part of humanized Fab H52
20307 ! part of a humanized anti-gamma-interferon Fab
20215 ! part of humanized Fab CTM01
20281 ! part of humanized anti-lysozyme Fv HuLys11
107489 !SQ NA # engineered antibody
76783 ! part of humanized anti-human Fas Fab HFE7A
20284 ! part of humanized anti-lysozyme Fv HuLys11
94676 ! part of humanized Fab D3H44 against human tissue factor
98630 ! part of anti-ERBb2 Fab Pertuzumab
87222 ! part of engineered Fab 2G12
20504 ! camelized monomeric VH
107890 !MQ NA P01857 # artificial chimera !SQ NA # Humanized antibody
73174 ! VHh CABAMD9 against alpha-amylase
73191 ! VHh CAB10 against alpha-amylase
85142 ! VHh against MazE addiction antidote
93398 ! anti-lysozyme Hl6 VHh domain
67279 ! anti-lysozyme VHh domain
67282 ! anti-lysozyme VHh domain
73185 ! VHh against alpha-amylase
20512 ! VHh of antibody cab-ca05
67275 ! anti-lysozyme VHh domain
20506 ! anti-lysozyme VHh domain
20510 ! anti-RNase A VHh domain
20513 ! cVH of antibody cab-ca05
109587 !SQ NA # camelid antibody 
105662 ! swapped dimer
20514 ! anti-gonadotropin alpha subunit VHh domain
61636 ! dye RR1-binding VHh domain
61638 ! dye RR1-binding VHh domain
20515 ! anti-RR6 VH domain
71199 ! VHh BRUC.D4.4
76216 ! anti-gonadotropin alpha subunit VHh domain
48933 ! sequences may differ within each classified species
60641 ! AV11S5-AJ17
20620 ! single-chain construct of beta and alpha N-domains connected by a 27-residue linker
77384 ! LC13 clone
79145 ! LC13 clone
20623 ! C-domain not seen in the crystal structure, due to disorder
20643 ! single-chain construct of beta and alpha N-domains connected by a 27-residue linker
77386 ! LC13 clone
79147 ! LC13 clone
72986 ! vbeta2.1
61975 ! b7-1 co-stimulatory complex
61949 ! b7-2 complex
89178 ! a triggering partner in natural cytotoxicity
105765 !SQ Q9NP99 21-133
19719 ! domain 1
19720 ! domain 1
19721 ! domain 1
98198 ! domain 1
19723 ! domain 1
19722 ! domain 1
19724 ! domain 1
19725 ! domain 1
98205 ! domain 1
19726 ! domain 1
19727 ! domain 1
63161 ! domain 1
19731 ! domains 1 and 3
19735 ! domains 1 and 3
19739 ! domains 1 and 3
19740 ! domain 3
19747 ! misfolded V (N-terminal) domain dimer
19749 ! misfolded V (N-terminal) domain dimer
19751 ! misfolded V (N-terminal) domain dimer
19757 ! misfolded V (N-terminal) domain dimer
48745 ! a soluble form of b7-1
61972 ! ctla-4 co-stimulatory complex
61947 ! complexed to ctla-4
63638 ! elaborated with insertions and N- and C-terminal extensions
105881 !SQ Q8AXI4 # fragment
106599 !SQ Q8AXI4 # fragment
108550 !SQ Q6X1E7 # fragment
108552 !SQ Q6X1E6 # fragment
20890 ! part of Fab 8F5
21142 ! part of Fab 28B4
21172 ! part of Fab D2.3
66649 ! part of Fab 36-71
21252 ! part of Diels-Alder catalytic Fab 13G5
21170 ! part of Fab D2.3
20998 ! part of Fab 4-4-20
21174 ! part of Fab D2.3
21190 ! part of hydrolytic antibody 6D9
72763 ! part of Fab D2.3
72768 ! part of Fab D2.3
21166 ! part of Fab MN14C11.6
21182 ! part of Fab D2.5
21146 ! part of Fab 184.1 against OspA
21098 ! part of anti-integrin Fab OPG2
20898 ! part of Fab 17/9
21184 ! part of Fab D2.5
21270 ! part of Fab 2E8 specific to the low density lipoprotein receptor binding region of apolipoprotein E
21192 ! part of hydrolytic antibody 6D9
20954 ! part of Fab J539
21002 ! part of Fab 36-71
74126 ! part of retro Diels-Alder catalytic Fab 9D9
21238 ! part of Fab M41 (artificial design)
74118 ! part of retro Diels-Alder catalytic Fab 9D9
20996 ! part of Fab TE33
21100 ! part of anti-integrin Fab OPG2
21176 ! part of Fab D2.3
21144 ! part of Fab 28B4
21092 ! part of Fab D44.1
21196 ! part of Fab F11.2.32 against HIV-1 protease
21152 ! part of Fab A5B7
21254 ! part of Fab TP7 against Taq DNA polymerase
21186 ! part of Fab D2.5
21072 ! part of Fab Jel 103
21096 ! part of Fab D44.1
21250 ! part of Diels-Alder catalytic Fab 1E9
21074 ! part of Fab Jel 103
21012 ! part of an anti-sweetener Fab
21070 ! part of Fab Jel 103
74134 ! part of retro Diels-Alder catalytic Fab 9D9
21086 ! part of an anti-cyclosporin A Fab
21076 ! part of Fab Jel 103
21020 ! part of Fab D1.3
21256 ! part of Fab TP7 against Taq DNA polymerase
21036 ! part of Fab NC41
21206 ! part of polysaccharide binding antibody 2H1
21188 ! part of Fab D2.5
21022 ! part of Fab D1.3
20930 ! part of Fab 26-10
21260 ! part of human rhinovirus 14 neutralizing Fab Mab1-IA
21024 ! part of D1.3 anti-idiotope Fab E225
21348 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
21034 ! part of Fab JE142
21068 ! part of Fab 17E8
72095 ! part of anti-human tissue factor Fab D3
21164 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
21112 ! part of a polysialic acid-binding Fab
21350 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
21200 ! part of Fab F11.2.32 against HIV-1 protease
21044 ! part of Fab 17-Ia
21228 ! part of anti-human tissue factor Fab 5G9
20992 ! part of Fab BV04-01
21038 ! part of Fab NC41
20932 ! part of Fab 26-10
20900 ! part of Fab 17/9
21028 ! part of Fab HyHEL-5
21026 ! part of Fab HyHEL-5
21018 ! part of Fab 26/9
20982 ! part of Fab Yst9.1
21088 ! part of Fab MoPC21
21082 ! part of Fab R6.5
21042 ! part of Fab NC41
21040 ! part of Fab NC41
21136 ! part of Fab MBR96
20970 ! part of Fab 50.1
20924 ! part of Fab B13I2
21090 ! part of Fab 40-50
20946 ! part of Fab R19.9
20948 ! part of Fab R19.9
21168 ! part of antibody against the melanoma associated gd2 ganglioside
20974 ! part of Fab 50.1
20870 ! part of intact IgG2a antibody Mab231
20888 ! part of Fab ANO2
74142 ! part of retro Diels-Alder catalytic Fab 9D9
21150 ! part of Fab LA-2 against OspA
20994 ! part of Fab BV04-01
21140 ! part of Fab 1583
20976 ! part of Fab 50.1
20908 ! part of Fab DB3
21240 ! part of Fab Desire-1
21138 ! part of Fab GH1002
20910 ! part of Fab DB3
20905 ! part of Fab 17/9; chain identifiers are mixed up
20914 ! part of Fab DB3
20912 ! part of Fab DB3
21030 ! part of Fab HyHEL-5
20892 ! part of Fab 8F5
21080 ! part of Fab F9.13.7
20926 ! part of Fab B13I2
20978 ! part of Fab 59.1
21222 ! part of Fab CTM01
21102 ! part of Fab N10
21106 ! part of Fab 409.5.3
21104 ! part of Fab 730.1.4
21234 ! part of Fab A6
21180 ! part of Fab D2.4
20958 ! part of Fab MCPC603
20918 ! part of Fab DB3
21014 ! part of an anti-sweetener Fab
20960 ! part of Fab MCPC603
20916 ! part of Fab DB3
20980 ! part of Fab 59.1
21084 ! part of neutralizing type 1 poliovirus Fab C3
20878 ! part of intact IgG1 antibody Mab61.1.3
20906 ! part of Fab 17/9
21066 ! part of Fab CNJ206
21232 ! part of anti-human tissue factor Fab 5G9
21000 ! part of Fab 4-4-20
21274 ! part of Fab 28 against HIV-1 RT
21162 ! part of Fab 25.3 against HIV-1 capsid protein (p24)
21016 ! part of catalytic antibody 1F7 with chorismate mutase activity
21110 ! part of Fab 409.5.3
21032 ! part of Fab HyHEL-10
21060 ! part of Fab CNJ206; H-chains in this entry seem to be mistraced in VH region
91305 ! part of the esterolytic Fab ms6-164
91260 ! part of Fab 29g12
85558 ! part of cationic cyclization catalytic Fab 4C6
97862 ! part of cationic cyclization catalytic Fab 4C6
97874 ! part of cationic cyclization catalytic Fab 4C6
97870 ! part of cationic cyclization catalytic Fab 4C6
96306 ! part of Fab s25-2
96302 ! part of Fab s25-2
97882 ! part of Diels-Alder catalytic Fab 13G5 
80624 ! part of anti-HCV Fab 19D9D6
91293 ! part of the esterolytic Fab ms6-164
96317 ! part of Fab s25-2
96017 ! part of anti-cocaine Fab M82G2
94288 ! part of anti-ssDNA Fab
96592 ! part of anti-cocaine Fab M82G2
96311 ! part of Fab s25-2
97858 ! part of cationic cyclization catalytic Fab 4C6
96325 ! part of Fab s45-18
66691 ! part of catalytic Fab 1D4
72318 ! part of anti-hepatitis B Fab pc282
95402 ! part of Fab Sya/J6
66695 ! part of catalytic Fab 1D4
21425 ! part of catalytic Fab 4B2
21392 ! part of anti-lysozyme Fab HYHEL-63
85537 ! part of anti-lysozyme Fab HYHEL-63
96297 ! part of Fab s45-18
21452 ! part of Fab 13B5 against HIV-1 capsid protein p24
21280 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
21352 ! part of anti-cytochrome c Fab E8
96929 ! part of Fab against potassium channel KcsA
97521 ! part of anti-cocaine Fab M82G2
97878 ! part of Diels-Alder catalytic Fab 13G5
85577 ! a part of Fab HYHEL-8
85542 ! part of anti-lysozyme Fab HYHEL-63
97866 ! part of cationic cyclization catalytic Fab 4C6
91301 ! part of the esterolytic Fab ms6-164
21400 ! part of anti-prion Fab 3F4
21342 ! part of anti-gp120 (HIV-1) Fab 58.2
21358 ! part of anti-HCG Fab 3A2
93921 ! part of anti-lysozyme Fab F10.6.6
97375 ! part of anti-cocaine Fab M82G2
91284 ! part of the esterolytic Fab ms6-164
59235 ! part of anti-TGFalpha Fab TAB2
68129 ! part of Fab against potassium channel KcsA
87350 ! part of anti-VD potassium channel KVAP Fab 33H1
97525 ! part of anti-cocaine Fab M82G2
21394 ! part of anti-lysozyme Fab HYHEL-63
59708 ! part of anti-IL2 Fab LNKB-2
79124 ! part of anti-HCV Fab 19D9D6
96277 ! part of Fab s25-2
66682 ! part of anti-estradiol Fab 57-2
21288 ! part of catalytic Fab 5C8
62542 ! part of anti-HIV Fab G3-519
77802 ! part of anti-testosterone Fab 77
59797 ! part of Fab RU5 inhibiting the collagen binding by the von willebrand factor a3 domain
59243 ! part of anti-TGFalpha Fab TAB2
83426 ! part of anti-angiogenin FAB; conflict: annotated in PDB as human
99146 ! part of blue fluorescent Fab 19G2
66083 ! part of anti-ssDNA Fab
85582 ! a part of Fab HYHEL-26
100856 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with a synthetic cyclic peptide
91273 ! part of the esterolytic Fab ms6-164
77798 ! part of anti-testosterone Fab 77
21406 ! part of Fab HGR-2 F6, a competitive antagonist of the glucagon receptor
91289 ! part of the esterolytic Fab ms6-164
21382 ! part of catalytic Fab 7C8
21290 ! part of catalytic Fab 5C8
21446 ! part of anti-C60 fullerene Fab
68134 ! part of Fab against potassium channel KcsA
72314 ! part of anti-hepatitis B Fab pc287
21282 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
77348 ! part of anti-photoproduct Fab 64M-2
21296 ! part of catalytic Fab 33F12 with an aldolase activity
21354 ! part of anti-cytochrome c Fab E8
96285 ! part of Fab s25-2
97854 ! part of cationic cyclization catalytic Fab 4C6
96927 ! part of Fab against potassium channel KcsA
66718 ! part of anti-estradiol Fab 57-2
21278 ! part of catalytic antibody 29G11 with esterase activity
21396 ! part of anti-lysozyme Fab HYHEL-63
96939 ! part of Fab against potassium channel KcsA
59712 ! part of anti-IL2 Fab LNKB-2
21356 ! part of anti-cytochrome c Fab E8
66280 ! part of anti-human Fas Fab hfe7a
84862 ! part of Fab specific for Y lipopolysaccharide
71147 ! part of anti-testosterone Fab
99154 ! part of blue fluorescent Fab 19G2
90425 ! part of anti-anti-idiotypic Fab against human angiotensin II, unliganded form 
97512 ! part of Fab 14F7
21458 ! part of anti-photoproduct Fab 64M-2
21364 ! part of Fab 6B5
21398 ! part of anti-FMDV Fab 4C4
21370 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
21292 ! part of catalytic Fab 5C8
72297 ! part of anti-hepatitis B Fab pc287; complex with ps1 peptide
84866 ! part of Fab specific for Y lipopolysaccharide
21372 ! part of antibody directed against the musk odorant traseolide
21451 ! part of blue fluorescent Fab 19G2
21402 ! part of anti-prion Fab 3F4
72310 ! part of anti-hepatitis B Fab pc282; complexed with ps1 peptide
85572 ! part of cationic cyclization catalytic Fab 4C6
71143 ! part of anti-testosterone Fab
21344 ! part of anti-gp120 (HIV-1) Fab 58.2
21284 ! part of Influenza virus hemagglutinin-neutralizing Fab
21346 ! part of anti-gp120 (HIV-1) Fab 58.2
21286 ! part of Influenza virus hemagglutinin-neutralizing Fab BH151
100457 ! part of anti-trombopoetin Fab tn1
21454 ! part of Fab 13B5 against HIV-1 capsid protein p24
83626 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
21428 ! part of Fab MAK33; conflict: annotated in PDB as human protein
72306 ! part of anti-hepatitis B Fab pc283; complexed with ps1 peptide
80117 ! part of anti-HCV Fab 19D9D6
21422 ! part of anti-Pres2 Fab F124
76651 ! part of anti-hepatitis B Fab (against PRES1 region)
100868 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with angiotensin II
96934 ! part of Fab against potassium channel KcsA
87424 ! part of anti-CLC chloride channel Fab
21388 ! part of Fab 1696 against HIV-1 protease
66959 ! part of anti-estradiol Fab 17E12E5
21456 ! part of Fab 13B5 against cytokine receptor common beta chain domain 4
84852 ! part of Fab specific for Y lipopolysaccharide
21294 ! part of an anti-E-selectin Fab
77368 ! part of anti-gibberellin A4 Fab 4-B8(8)/E9; conflict: annotated in PDB as human protein
91760 ! part of Fab 83.1 against HIV-1 gp120 
21324 ! part of anti-P-glycoprotein Fab MRK-16
21326 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21330 ! part of anti-gp120 (HIV-1) Fab CB 4-1
66963 ! part of anti-estradiol Fab 17E12E5
21332 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21328 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21336 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21334 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21338 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21404 ! part of the cytochrome P450-arom activity suppressing Fab 32C2
21340 ! part of anti-gp120 (HIV-1) Fab CB 4-1
86755 ! part of anti-Pf MSP1 Fab
21436 ! part of anti-bet v1 Fab BV16
87345 ! part of anti-VD potassium channel KVAP Fab 6E1
100475 ! part of anti-trombopoetin Fab tn1
99059 ! part of Fab 28 against HIV-1 RT
80063 ! part of Fab 28 against HIV-1 RT
61421 ! part of Fab 28 against HIV-1 RT
21378 ! part of Fab R24 from murine ascites
80210 ! part of Fab 28 against HIV-1 RT
87444 ! part of anti-CLC chloride channel Fab
71574 ! part of Fab 28 against HIV-1 RT
72386 ! part of Fab against influenza virus hemagglutinin
87434 ! part of anti-CLC chloride channel Fab !SQ P01837 #! KAC_MOUSE Ig kappa chain C region
106552 !SQ P01837 #! KAC_MOUSE Ig kappa chain C region
104682 !SQ NA # part of Fab 28 against HIV-1 RT 
108173 !MQ P03976 P01837 #! natural chimera !SQ P01837 # KAC_MOUSE (P01837) Ig kappa chain C region
108163 !MQ P03976 P01837 #! natural chimera !SQ P01837 # KAC_MOUSE (P01837) Ig kappa chain C region
106116 !MQ P04940 P01837 # natural chimera !SQ P01837 # KAC_MOUSE Ig kappa chain C region
105275 !MQ P06310 P01837  !SQ P01837 # KAC_MOUSE Ig kappa chain C region
73959 ! part of anti-IL-10 Fab 9D7
21386 ! part of antibody against the main immunogenic region of the human muscle acetylcholine receptor
21308 ! part of therapeutic monoclonal antibody CAMPATH-1G
59889 ! part of Fab 198 against acetylcholine receptor
88569 ! including humanized antibodies (chimeric proteins with human constant domains)
21438 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
73659 ! part of humanized anti-ERBb2 Fab 2C4
67054 ! part of humanized Fab D3H44 against human tissue factor
91535 ! part of an anti HIV-1 Fab
67048 ! part of humanized Fab D3H44 against human tissue factor
80253 ! part of metal chelatase catalytic Fab 7G12; germline antibody; chain identifiers are probably mixed up
87213 ! part of Fab 2G12
98136 ! part of anti HIV-1 gp120-reactive Fab 48D
98161 ! part of anti HIV-1 gp120-reactive Fab 412D
62645 ! part of Fab BO2C11 against the C2 domain of factor VIII
21126 ! part of humanized Fab TR1.9
97478 ! part of HIV-1 neutralizing Fab x5
21310 ! part of humanized therapeutic antibody CAMPATH-1H
88509 ! part of HIV-1 neutralizing Fab 2F5
21440 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
21210 ! part of humanized oxy-cope catalytic Fab az-28
21212 ! part of humanized oxy-cope catalytic Fab az-28
21114 ! part of humanized Fab 48G7
21116 ! part of humanized Fab 48G7
88505 ! part of HIV-1 neutralizing Fab 2F5
21118 ! part of humanized Fab 48G7
65016 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
20936 ! part of Fab Kau cold agglutinin IgM
21368 ! part of metal chelatase catalytic Fab 7G12; mature antibody
87066 ! part of Fab 2G12
61924 ! part of humanized Fab GNC92H2
20964 ! part of humanized Fab 4D5, herceptin
98142 ! part of anti HIV-1 gp120-reactive Fab 17B
21156 ! part of humanized Fab A5B7
21374 ! part of humanized Fab R24 from murine ascites
21320 ! part of humanized Fab-12 neutralizing VEGF; affinity matured
21132 ! part of humanized Fab CBR96
21120 ! part of humanized Fab 48G7
21248 ! part of humanized Diels-Alder catalytic Fab
21262 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
107484 !SQ NA # engineered antibody
98204 ! part of anti HIV-1 gp120-reactive Fab 17B
20968 ! part of humanized Fab 4D5, herceptin
21158 ! part of CD25-binding humanized Fab CHI621
20920 ! part of Fab 3D6
60988 ! part of IgM RF 2A2
21264 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
21412 ! part of IgM RF 2A2
21511 ! part of Bence-Jones protein DEL
21134 ! part of humanized Fab CBR96
80319 ! part of humanized Fab 4D5, herceptin
21244 ! part of humanized Diels-Alder catalytic Fab
84970 ! part of humanized anti-alpha1 integrin I-domain Fab
21216 ! part of humanized oxy-cope catalytic Fab az-28
65024 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
100120 ! part of catalytic Fab 14d9
21226 ! part of humanized Fab CTM01
21298 ! part of a humanized anti-gamma-interferon Fab
20956 ! part of humanized Fab H52
100112 ! part of catalytic Fab 14d9
20894 ! part of humanized Fab B72.3
20940 ! part of Fab Kau cold agglutinin IgM
61448 ! part of intact IgG B12 antibody
107488 !SQ NA # engineered antibody
76786 ! part of humanized anti-human Fas Fab HFE7A
21316 ! part of humanized Fab-12 neutralizing VEGF
21220 ! part of humanized oxy-cope catalytic Fab az-28
98211 ! part of anti HIV-1 gp120-reactive Fab 17B
21266 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
94681 ! part of humanized Fab D3H44 against human tissue factor
88154 ! part of humanized Fab 8-18c5
98195 ! part of anti HIV-1 gp120-reactive Fab 47E
71162 ! part of Fab 5C8 against C40 ligand
98629 ! part of anti-ERBb2 Fab Pertuzumab
21312 ! part of antibody to CAMPATH-1H humanized Fab
87221 ! part of Fab 2G12
80501 ! part of metal chelatase catalytic Fab 7G12; chimeric germline antibody
85709 ! part of metal chelatase catalytic Fab 7G12; chimeric germline antibody
105240 !MQ NA  # artificial chimera !SQ  P01834 # KAC_HUMAN Ig kappa chain C region.
107889 !MQ NA P01834 # artificial chimera !SQ P01834 # KAC_HUMAN Ig kappa chain C region
80497 ! part of metal chelatase catalytic Fab 7G12; chimeric mature antibody
21300 ! part of a chimeric anti-gamma-interferon Fab
80495 ! part of metal chelatase catalytic Fab 7G12; chimeric affinity matured antibody
20988 ! part of Fab SE155-4
20986 ! part of Fab SE155-4
20984 ! part of Fab SE155-4
21360 ! part of tumor-specific Fab SM3 against epithelial mucin Muc1
20990 ! part of Fab SE155-4
21414 ! part of anti-carbohydrate Fab S-20-4
20942 ! part of Fab Cha255
21004 ! part of Fab HC19
21416 ! part of anti-carbohydrate Fab S-20-4
21122 ! part of Fab N1G9
21124 ! part of Fab N1G9
20944 ! part of Fab Cha255
66952 ! part of anti-estradiol Fab 10G6D6
66924 ! part of anti-estradiol Fab 10G6D6
21008 ! part of Fab HC19
21010 ! part of Fab HC19
21418 ! part of anti-carbohydrate Fab S-20-4
21444 ! part of anti-sweetener Fab NC10.14
21130 ! part of an anti-nitrophenol Fab
21006 ! part of Fab HC19
95520 ! part of anti-morphine Fab 9b1
98153 ! part of anti HIV-1 gp120-reactive Fab E51
20884 ! part of Fab HIL
21208 ! part of Fab B7-15A2
20950 ! part of Fab KOL
20886 ! part of Fab NEW
95524 ! part of anti-morphine Fab 9b1
84611 ! part of amyloidogenic protein BUR
71900 ! part of amyloidogenic protein BUR
91786 ! part of Fab 2d12.5
84615 ! part of amyloidogenic protein BUR
91794 ! part of Fab 2d12.5
21473 ! part of the antibody MCG light chain dimer
91948 ! part of Fab 10c12 against factor IX Gla domain 
21461 ! part of Bence-Jones protein LOC
21475 ! part of the antibody MCG light chain dimer
21463 ! part of Bence-Jones protein LOC
91904 ! part of cocaine hydrolytic Fab 15a10
21465 ! part of Bence-Jones protein LOC
21477 ! part of the antibody MCG light chain dimer
95588 ! part of anti HIV-1 Fab 447-52d
21481 ! part of the antibody MCG light chain dimer
21479 ! part of the antibody MCG light chain dimer
21483 ! part of the antibody MCG light chain dimer
21487 ! part of the antibody MCG light chain dimer
21485 ! part of the antibody MCG light chain dimer
21489 ! part of the antibody MCG light chain dimer
21491 ! part of the antibody MCG light chain dimer
21467 ! part of Bence-Jones protein CLE
21495 ! part of the antibody MCG light chain dimer
21497 ! part of the antibody MCG light chain dimer
21493 ! part of the antibody MCG light chain dimer
20952 ! part of antibody KOL; intact protein but only Fab's can be seen in the crystal structure
21499 ! part of the antibody MCG light chain dimer
21272 ! part of IgM rheumatoid factor Fab
21503 ! part of the antibody MCG light chain dimer
21501 ! part of the antibody MCG light chain dimer
94687 ! part of Fab 6A6
21505 ! part of the antibody MCG light chain dimer
21509 ! part of heterologous L chain dimer MCG-WEIR
21468 ! part of intact antibody MCG
21204 ! part of Fab H57
88575 ! including humanized antibodies (chimeric proteins with human constant domains)
21439 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
98151 ! part of anti HIV-1 gp120-reactive Fab E51
73657 ! part of humanized anti-ERBb2 Fab 2C4
20885 ! part of Fab HIL
67052 ! part of humanized Fab D3H44 against human tissue factor
91531 ! part of an anti HIV-1 Fab
80255 ! part of metal chelatase catalytic Fab 7G12; germline antibody; chain identifiers are probably mixed up
67046 ! part of humanized Fab D3H44 against human tissue factor
87215 ! part of Fab 2G12
20887 ! part of Fab NEW
21209 ! part of Fab B7-15A2
20951 ! part of Fab KOL
98159 ! part of anti HIV-1 gp120-reactive Fab 412D
98134 ! part of anti HIV-1 gp120-reactive Fab 48D
62647 ! part of Fab BO2C11 against the C2 domain of factor VIII
21127 ! part of humanized Fab TR1.9
97480 ! part of HIV-1 neutralizing Fab x5
21311 ! part of humanized therapeutic antibody CAMPATH-1H
88507 ! part of HIV-1 neutralizing Fab 2F5
21441 ! part of humanized catalytic Fab 21D8 with a decarboxylase activity
21211 ! part of humanized oxy-cope catalytic Fab az-28
21213 ! part of humanized oxy-cope catalytic Fab az-28
21115 ! part of humanized Fab 48G7
21117 ! part of humanized Fab 48G7
21119 ! part of humanized Fab 48G7
88503 ! part of HIV-1 neutralizing Fab 2F5
65018 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
91946 ! part of Fab 10c12 against factor IX Gla domain 
87062 ! part of Fab 2G12
21369 ! part of metal chelatase catalytic Fab 7G12; mature antibody
20965 ! part of humanized Fab 4D5, herceptin
61926 ! part of humanized Fab GNC92H2
98144 ! part of anti HIV-1 gp120-reactive Fab 17B
21157 ! part of humanized Fab A5B7
21375 ! part of humanized Fab R24 from murine ascites
21133 ! part of humanized Fab CBR96
21321 ! part of humanized Fab-12 neutralizing VEGF; affinity matured
21121 ! part of humanized Fab 48G7
21263 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
21249 ! part of humanized Diels-Alder catalytic Fab
107482 !SQ NA # engineered antibody
98202 ! part of anti HIV-1 gp120-reactive Fab 17B
20921 ! part of Fab 3D6
20969 ! part of humanized Fab 4D5, herceptin
21159 ! part of CD25-binding humanized Fab CHI621
95584 ! part of anti HIV-1 Fab 447-52d
21265 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
80321 ! part of humanized Fab 4D5, herceptin
21135 ! part of humanized Fab CBR96
84968 ! part of humanized anti-alpha1 integrin I-domain Fab
21217 ! part of humanized oxy-cope catalytic Fab az-28
65026 ! part of humanized catalytic Fab 28b4 with a sulfide oxidase activity
21245 ! part of humanized Diels-Alder catalytic Fab
100122 ! part of catalytic Fab 14d9
21227 ! part of humanized Fab CTM01
20957 ! part of humanized Fab H52
21299 ! part of a humanized anti-gamma-interferon Fab
100114 ! part of catalytic Fab 14d9
20895 ! part of humanized Fab B72.3
61442 ! part of intact IgG B12 antibody
107490 !SQ NA # engineered antibody
76784 ! part of humanized anti-human Fas Fab HFE7A
21317 ! part of humanized Fab-12 neutralizing VEGF
20953 ! part of antibody KOL; intact protein but only Fab's can be seen in the crystal structure
21221 ! part of humanized oxy-cope catalytic Fab az-28
98209 ! part of anti HIV-1 gp120-reactive Fab 17B
21267 ! part of HIV-1 neutralizing Fab 17B; binds to the CD4-induced state of gp120
94677 ! part of humanized Fab D3H44 against human tissue factor
88156 ! part of humanized Fab 8-18c5
98197 ! part of anti HIV-1 gp120-reactive Fab 47E
98631 ! part of anti-ERBb2 Fab Pertuzumab
71160 ! part of Fab 5C8 against C40 ligand
21313 ! part of antibody to CAMPATH-1H humanized Fab
87223 ! part of Fab 2G12
21469 ! part of intact antibody MCG
80503 ! part of metal chelatase catalytic Fab 7G12;chimeric germline antibody
85707 ! part of metal chelatase catalytic Fab 7G12; chimeric affinity matured antibody
105238 !MQ NA P01857 # artificial chimera !SQ P01857 # IGHG1_HUMAN Ig gamma-1 chain C region
107891 !MQ NA P01857 # artificial chimera !SQ P01857 # IGHG1_HUMAN Ig gamma-1 chain C region
80499 ! part of metal chelatase catalytic Fab 7G12; chimeric mature antibody
21301 ! part of a chimeric anti-gamma-interferon Fab
80493 ! part of metal chelatase catalytic Fab 7G12; chimeric affinity matured antibody
91303 ! part of the esterolytic Fab ms6-164
91258 ! part of Fab 29g12
85556 ! part of cationic cyclization catalytic Fab 4C6
97860 ! part of cationic cyclization catalytic Fab 4C6
97872 ! part of cationic cyclization catalytic Fab 4C6
97868 ! part of cationic cyclization catalytic Fab 4C6
96308 ! part of Fab s25-2 
96304 ! part of Fab s25-2 
97880 ! part of Diels-Alder catalytic Fab 13G5
80622 ! part of anti-HCV Fab 19D9D6
91291 ! part of the esterolytic Fab ms6-164
95518 ! part of anti-morfine Fab 9b1
96319 ! part of Fab s25-2 
96015 ! part of anti-cocaine Fab M82G2
96590 ! part of anti-cocaine Fab M82G2
94290 ! part of anti-ssDNA Fab
96313 ! part of Fab s25-2 
97856 ! part of cationic cyclization catalytic Fab 4C6
96327 ! part of Fab s45-18 
66689 ! part of catalytic Fab 1D4
72316 ! part of anti-hepatitis B Fab pc282
85539 ! part of anti-lysozyme Fab HYHEL-63
66693 ! part of catalytic Fab 1D4
21393 ! part of anti-lysozyme Fab HYHEL-63
21427 ! part of catalytic Fab 4B2
96299 ! part of Fab s45-18 
21353 ! part of anti-cytochrome c Fab E8
21281 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
21453 ! part of Fab 13B5 against HIV-1 capsid protein p24
97519 ! part of anti-cocaine Fab M82G2
96931 ! part of Fab against potassium channel KcsA
97876 ! part of Diels-Alder catalytic Fab 13G5
85579 ! a part of Fab HYHEL-8
21143 ! part of Fab 28B4
85544 ! part of anti-lysozyme Fab HYHEL-63
20891 ! part of Fab 8F5
97864 ! part of cationic cyclization catalytic Fab 4C6
95522 ! part of anti-morfine Fab 9b1
91299 ! part of the esterolytic Fab ms6-164
21343 ! part of anti-gp120 (HIV-1) Fab 58.2
21401 ! part of anti-prion Fab 3F4
21171 ! part of Fab D2.3
21253 ! part of Diels-Alder catalytic Fab 13G5
66647 ! part of Fab 36-71
21359 ! part of anti-HCG Fab 3A2
21173 ! part of Fab D2.3
93923 ! part of anti-lysozyme Fab F10.6.6
91282 ! part of the esterolytic Fab ms6-164
97373 ! part of anti-cocaine Fab M82G2
68127 ! part of Fab against potassium channel KcsA
21167 ! part of Fab MN14C11.6
21191 ! part of hydrolytic antibody 6D9
20999 ! part of Fab 4-4-20
87352 ! part of anti-VD potassium channel KVAP Fab 33H1
21175 ! part of Fab D2.3
20989 ! part of Fab SE155-4
20987 ! part of Fab SE155-4
20985 ! part of Fab SE155-4
59233 ! part of anti-TGFalpha Fab TAB2
72766 ! part of Fab D2.3
72761 ! part of Fab D2.3
97523 ! part of anti-cocaine Fab M82G2
21183 ! part of Fab D2.5
20899 ! part of Fab 17/9
59706 ! part of anti-IL2 Fab LNKB-2
21185 ! part of Fab D2.5
21099 ! part of anti-integrin Fab OPG2
79126 ! part of anti-HCV Fab 19D9D6
21395 ! part of anti-lysozyme Fab HYHEL-63
21147 ! part of Fab 184.1 against OspA
21271 ! part of Fab 2E8 specific to the low density lipoprotein receptor binding region of apolipoprotein E
96279 ! part of Fab s25-2 
21239 ! part of Fab M41 (artificial design)
21003 ! part of Fab 36-71
21361 ! part of tumor-specific Fab SM3 against epithelial mucin Muc1
21193 ! part of hydrolytic antibody 6D9
21289 ! part of catalytic Fab 5C8
66680 ! part of anti-estradiol Fab 57-2
74116 ! part of retro Diels-Alder catalytic Fab 9D9
20991 ! part of Fab SE155-4
74124 ! part of retro Diels-Alder catalytic Fab 9D9
62540 ! part of anti-HIV Fab G3-519
59239 ! part of anti-TGFalpha Fab TAB2
20997 ! part of Fab TE33
83428 ! part of anti-angiogenin FAB; conflict: annotated in PDB as human
77800 ! part of anti-testosterone Fab 77
21101 ! part of anti-integrin Fab OPG2
59791 ! part of Fab RU5 inhibiting the collagen binding by the von willebrand factor a3 domain
99144 ! part of blue fluorescent Fab 19G2
91788 ! part of Fab 2d12.5
66085 ! part of anti-ssDNA Fab
21177 ! part of Fab D2.3
21145 ! part of Fab 28B4
85584 ! a part of Fab HYHEL-26
100854 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with a synthetic cyclic peptide
91271 ! part of the esterolytic Fab ms6-164
21197 ! part of Fab F11.2.32 against HIV-1 protease
21407 ! part of Fab HGR-2 F6, a competitive antagonist of the glucagon receptor
77796 ! part of anti-testosterone Fab 77
21153 ! part of Fab A5B7
21093 ! part of Fab D44.1
21255 ! part of Fab TP7 against Taq DNA polymerase
91287 ! part of the esterolytic Fab ms6-164
91796 ! part of Fab 2d12.5
21447 ! part of anti-C60 fullerene Fab
21097 ! part of Fab D44.1
68132 ! part of Fab against potassium channel KcsA
72312 ! part of anti-hepatitis B Fab pc287
21383 ! part of catalytic Fab 7C8
21415 ! part of anti-carbohydrate Fab S-20-4
21251 ! part of Diels-Alder catalytic Fab 1E9
21291 ! part of catalytic Fab 5C8
21187 ! part of Fab D2.5
21283 ! part of Fab NMC-4 blocking the von willebrand factor (vwf) a1 domain function
21073 ! part of Fab Jel 103
77346 ! part of anti-photoproduct Fab 64M-2
21355 ! part of anti-cytochrome c Fab E8
21075 ! part of Fab Jel 103
21071 ! part of Fab Jel 103
21013 ! part of an anti-sweetener Fab
21297 ! part of catalytic Fab 33F12 with an aldolase activity
97852 ! part of cationic cyclization catalytic Fab 4C6
96925 ! part of Fab against potassium channel KcsA
96287 ! part of Fab s25-2 
21087 ! part of an anti-cyclosporin A Fab
21279 ! part of catalytic antibody 29G11 with esterase activity
21397 ! part of anti-lysozyme Fab HYHEL-63
21077 ! part of Fab Jel 103
66716 ! part of anti-estradiol Fab 57-2
20943 ! part of Fab Cha255
74132 ! part of retro Diels-Alder catalytic Fab 9D9
96941 ! part of Fab against potassium channel KcsA
21357 ! part of anti-cytochrome c Fab E8
59710 ! part of anti-IL2 Fab LNKB-2
21417 ! part of anti-carbohydrate Fab S-20-4
71145 ! part of anti-testosterone Fab
66278 ! part of anti-human Fas Fab hfe7a
21005 ! part of Fab HC19
90423 ! part of anti-anti-idiotypic Fab against human angiotensin II, unliganded form 
97510 ! part of Fab 14F7
99152 ! part of blue fluorescent Fab 19G2
21207 ! part of polysaccharide binding antibody 2H1P
21257 ! part of Fab TP7 against Taq DNA polymerase
21189 ! part of Fab D2.5
21365 ! part of Fab 6B5
21459 ! part of anti-photoproduct Fab 64M-2
21021 ! part of Fab D1.3
21037 ! part of Fab NC41
21123 ! part of Fab N1G9
21399 ! part of anti-FMDV Fab 4C4
21025 ! part of D1.3 anti-idiotope Fab E225
21261 ! part of human rhinovirus 14 neutralizing Fab Mab1-IA
20931 ! part of Fab 26-10
21023 ! part of Fab D1.3
21349 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
21371 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
21035 ! part of Fab JE142
21113 ! part of a polysialic acid-binding Fab
72093 ! part of anti-human tissue factor Fab D3
21293 ! part of catalytic Fab 5C8
21351 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
21165 ! part of bactericidal Fab MN12H2 against Neisseria meningitidis
21069 ! part of Fab 17E8
91902 ! part of cocaine hydrolytic Fab 15a10
21125 ! part of Fab N1G9
72308 ! part of anti-hepatitis B Fab pc282
21229 ! part of anti-human tissue factor Fab 5G9
21045 ! part of Fab 17-Ia
21450 ! part of blue fluorescent Fab 19G2
20933 ! part of Fab 26-10
72295 ! part of anti-hepatitis B Fab pc287; complex with ps1 peptide ! against PRES1 region
21373 ! part of antibody directed against the musk odorant traseolide
21403 ! part of anti-prion Fab 3F4
21201 ! part of Fab F11.2.32 against HIV-1 protease
21039 ! part of Fab NC41
20993 ! part of Fab BV04-01
20901 ! part of Fab 17/9
85574 ! part of cationic cyclization catalytic Fab 4C6
21027 ! part of Fab HyHEL-5
21029 ! part of Fab HyHEL-5
71141 ! part of anti-testosterone Fab
21043 ! part of Fab NC41
21041 ! part of Fab NC41
21083 ! part of Fab R6.5
21089 ! part of Fab MoPC21
20983 ! part of Fab Yst9.1
21345 ! part of anti-gp120 (HIV-1) Fab 58.2
21019 ! part of Fab 26/9
21169 ! part of antibody against the melanoma associated gd2 ganglioside
20925 ! part of Fab B13I2
21285 ! part of Influenza virus hemagglutinin-neutralizing Fab
20945 ! part of Fab Cha255
20947 ! part of Fab R19.9
20949 ! part of Fab R19.9
20971 ! part of Fab 50.1
21347 ! part of anti-gp120 (HIV-1) Fab 58.2
21287 ! part of Influenza virus hemagglutinin-neutralizing Fab BH151
21091 ! part of Fab 40-50
100453 ! part of anti-trombopoetin Fab tn1
20975 ! part of Fab 50.1
20889 ! part of Fab ANO2
20871 ! part of intact IgG2a antibody Mab231
83628 ! part of catalytic Fab HA-19A4 with a polyene cyclase activity
20977 ! part of Fab 50.1
21141 ! part of Fab 1583
20995 ! part of Fab BV04-01
74140 ! part of retro Diels-Alder catalytic Fab 9D9
21151 ! part of Fab LA-2 against OspA
21455 ! part of Fab 13B5 against HIV-1 capsid protein p24
21429 ! part of Fab MAK33; conflict: annotated in PDB as human protein
72304 ! part of anti-hepatitis B Fab pc283; complexed with ps1 peptide
66954 ! part of anti-estradiol Fab 10G6D6
20911 ! part of Fab DB3
21423 ! part of anti-Pres2 Fab F124
21139 ! part of Fab GH1002
21241 ! part of Fab Desire-1
20909 ! part of Fab DB3
80115 ! part of anti-HCV Fab 19D9D6
100866 ! part of anti-anti-idiotypic Fab against human angiotensin II, complex with angiotensin II
96936 ! part of Fab against potassium channel KcsA
20904 ! part of Fab 17/9; chain identifiers are mixed up
21031 ! part of Fab HyHEL-5
66926 ! part of anti-estradiol Fab 10G6D6
20915 ! part of Fab DB3
21389 ! part of Fab 1696 against HIV-1 protease
87422 ! part of anti-CLC chloride channel Fab
20913 ! part of Fab DB3
20893 ! part of Fab 8F5
66957 ! part of anti-estradiol Fab 17E12E5
77364 ! part of anti-gibberellin A4 Fab 4-B8(8)/E9; conflict: annotated in PDB as human protein
21081 ! part of Fab F9.13.7
20979 ! part of Fab 59.1
21457 ! part of Fab 13B5 against cytokine receptor common beta chain domain 4
20927 ! part of Fab B13I2
21295 ! part of an anti-E-selectin Fab
21009 ! part of Fab HC19
91756 ! part of Fab 83.1 against HIV-1 gp120 
21107 ! part of Fab 409.5.3
21011 ! part of Fab HC19
21325 ! part of anti-P-glycoprotein Fab MRK-16
21327 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21181 ! part of Fab D2.4
21223 ! part of Fab CTM01
21235 ! part of Fab A6
21105 ! part of Fab 730.1.4
21103 ! part of Fab N10
21333 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21331 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21015 ! part of an anti-sweetener Fab
21329 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20917 ! part of Fab DB3
20919 ! part of Fab DB3
20981 ! part of Fab 59.1
66961 ! part of anti-estradiol Fab 17E12E5
21445 ! part of anti-sweetener Fab NC10.14
21131 ! part of an anti-nitrophenol Fab
21337 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21419 ! part of anti-carbohydrate Fab S-20-4
94689 ! part of Fab 6A6
21233 ! part of anti-human tissue factor Fab 5G9
21339 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21335 ! part of anti-gp120 (HIV-1) Fab CB 4-1
20907 ! part of Fab 17/9
21067 ! part of Fab CNJ206
21085 ! part of neutralizing type 1 poliovirus Fab C3
20879 ! part of intact IgG1 antibody Mab61.1.3
21405 ! part of the cytochrome P450-arom activity suppressing Fab 32C2
86757 ! part of anti-Pf MSP1 Fab
21341 ! part of anti-gp120 (HIV-1) Fab CB 4-1
21437 ! part of anti-bet v1 Fab BV16
21275 ! part of Fab 28 against HIV-1 RT
21001 ! part of Fab 4-4-20
87347 ! part of anti-VD potassium channel KVAP Fab 6E1
100467 ! part of anti-trombopoetin Fab tn1
99057 ! part of Fab 28 against HIV-1 RT
21163 ! part of Fab 25.3 against HIV-1 capsid protein (p24)
21017 ! part of catalytic antibody 1F7 with chorismate mutase activity
21111 ! part of Fab 409.5.3
80061 ! part of Fab 28 against HIV-1 RT
21007 ! part of Fab HC19
21033 ! part of Fab HyHEL-10
61423 ! part of Fab 28 against HIV-1 RT
80208 ! part of Fab 28 against HIV-1 RT
87442 ! part of anti-CLC chloride channel Fab
71572 ! part of Fab 28 against HIV-1 RT
72384 ! part of Fab against influenza virus hemagglutinin
87432 ! part of anti-CLC chloride channel Fab
21061 ! part of Fab CNJ206; H-chains in this entry seem to be mistraced in VH region !SQ P01868 #! GC1_MOUSE Ig gamma-1 chain C region secreted form
106550 !SQ P01868 #! GC1_MOUSE Ig gamma-1 chain C region secreted form
104680 !SQ NA # part of Fab 28 against HIV-1 RT 
106114 !MQ P01750 P01863 # natural chimera !SQ P01863 # GCAA_MOUSE Ig gamma-2A chain C region, A allele
107216 !MQ P01631 P01837 #! natural chimera !SQ P01837 # KAC_MOUSE (P01837) Ig kappa chain C region
107193 !MQ P01631 P01837 #! natural chimera !SQ P01837 # KAC_MOUSE (P01837) Ig kappa chain C region
107214 !MQ P06327 P01864 #! natural chimera !SQ P01864 # GCAB_MOUSE (P01864) Ig gamma-2A chain C region
107191 !MQ P06327 P01864 #! natural chimera !SQ P01864 # GCAB_MOUSE (P01864) Ig gamma-2A chain C region
105273 !MQ P18532 P01868 # natural 'chimera' !SQ P01868 # GC1_MOUSE Ig gamma-1 chain C region secreted form
107221 !MQ P01631 P01837 #! natural chimera !SQ P01837 # KAC_MOUSE (P01837) Ig kappa chain C region
107219 !MQ P06327 P01864 #! natural chimera !SQ P01864 # GCAB_MOUSE (P01864) Ig gamma-2A chain C region
95404 ! part of Fab Sya/J6
84864 ! part of Fab specific for Y lipopolysaccharide
84868 ! part of Fab specific for Y lipopolysaccharide
21137 ! part of Fab MBR96 ! from murine ascites
84854 ! part of Fab specific for Y lipopolysaccharide
21379 ! part of Fab R24 from murine ascites
108171 !MQ P01811 P22436 #! natural chimera !SQ P22436 # GC3_MOUSE (P22436) Ig gamma-3 chain C region
108165 !MQ P01811 P22436 #! natural chimera !SQ P22436 # GC3_MOUSE (P22436) Ig gamma-3 chain C region
73955 ! part of anti-IL-10 Fab 9D7
21387 ! part of antibody against the main immunogenic region of the human muscle acetylcholine receptor
21309 ! part of therapeutic monoclonal antibody CAMPATH-1G
59891 ! part of Fab 198 against acetylcholine receptor
21205 ! part of Fab H57
20955 ! part of Fab J539
20959 ! part of Fab MCPC603
20961 ! part of Fab MCPC603
20937 ! part of Fab Kau cold agglutinin IgM
21413 ! part of IgM rheumatoid factor Fab
60990 ! part of IgM rheumatoid factor Fab
20941 ! part of Fab Kau cold agglutinin IgM
21273 ! part of IgM rheumatoid factor Fab
73642 ! part of a Fc
87315 ! part of a Fc
21514 ! part of a Fc
87327 ! part of a Fc
76659 ! part of a Fc
76655 ! part of a Fc
61443 ! part of intact IgG B12 antibody
90604 ! part of a Fc
21518 ! part of a Fc
21516 ! part of a Fc
21522 ! part of a Fc
62456 ! part of a Fc
76665 ! part of a Fc
76663 ! part of a Fc
106659 !SQ P01857 118-327 # GC1_HUMAN Ig gamma-1 chain C region
62464 ! part of a Fc
21470 ! part of intact antibody MCG
21544 ! part of a Fc
21528 ! part of a Fc
21524 ! part of a Fc
76669 ! part of a Fc
106645 !SQ P01857 #118-327
20880 ! part of intact IgG1 antibody Mab61.1.3
20872 ! part of intact IgG2a antibody Mab231
21538 ! part of a Fc
21542 ! part of a Fc
73643 ! part of a Fc
87316 ! part of a Fc
21515 ! part of a Fc
87328 ! part of a Fc
76660 ! part of a Fc
76656 ! part of a Fc
61444 ! part of intact IgG B12 antibody
90605 ! part of a Fc
21519 ! part of a Fc
21517 ! part of a Fc
21523 ! part of a Fc
62457 ! part of a Fc
76666 ! part of a Fc
76664 ! part of a Fc
106660 !SQ P01857 118-327 # GC1_HUMAN Ig gamma-1 chain C region
62465 ! part of a Fc
21471 ! part of intact antibody MCG
21545 ! part of a Fc
21529 ! part of a Fc
21525 ! part of a Fc
76670 ! part of a Fc
106646 !SQ P01857 #118-327
21548 ! CH-gamma-3 domain only from antibody MAK33
20881 ! part of intact IgG1 antibody Mab61.1.3
20873 ! part of intact IgG2a antibody Mab231
21539 ! part of a Fc
21543 ! part of a Fc
21546 ! CH-gamma-3 domain only
21535 ! polysaccharide binding antibody
77385 ! LC13 clone
79146 ! LC13 clone
77387 ! LC13 clone
79148 ! LC13 clone
73858 ! beta2-microglobulin only
104601 !SQ P01884
104564 !SQ P01884
20863 ! conflict: annotated in PDB as mouse protein
20669 ! CA-atoms only
66955 ! beta2-microglobulin only
105393 !SQ P61769 21-119
105399 !SQ P61769 21-119
105396 !SQ P61769 21-119
104299 !SQ P01887
104599 !SQ P13746 25-299 # 1A11_HUMAN HLA class I histocompatibility antigen, A-11 alpha chain precursor
104562 !SQ P13746 25-299 # 1A11_HUMAN HLA class I histocompatibility antigen, A-11 alpha chain precursor
20668 ! CA-atoms only
105391 !SQ P01892 25-298
105397 !SQ P01892 25-298
105394 !SQ P01892 25-298
48965 ! fat depleting factor related to class I MHC
88610 ! gamma, delta T-cell ligand
88619 ! probably orthologous to the mouse H2-DM
88620 ! probably orthologous to the human HLA-DM
88621 ! probably orthologous to the mouse I-E group
105648 !SQ P01903 28-207
105640 !SQ P01903 28-207
106489 !SQ P01903 28-207
106485 !SQ P01903 28-207
88622 ! probably orthologous to the human HLA-DR group
88623 ! probably orthologous to the mouse I-A group
100062 ! complexed with a hypocretin peptide
98764 ! complexed with deamidated gliadin peptide
63145 ! complexed with a human insulin peptide
88624 ! probably orthologous to the human HLA-DQ group
21639 ! contains covalently bound peptides
21643 ! contains covalently bound peptides
88626 ! probably orthologous to the mouse H2-DM
88627 ! probably orthologous to the human HLA-DM
88628 ! probably orthologous to the mouse I-E group
105650 !SQ P04229 30-219
105642 !SQ P04229 30-219
106491 !SQ P04229 30-219
106487 !SQ P04229 30-219
88629 ! probably orthologous to the human HLA-DR group
59910 ! contains covalently bound peptides at the N-termini of chains B and D
59902 ! contains covalently bound peptides at the N-termini of chains B and D
21634 ! contains covalently bound peptides at the N-termini of chains B and D
61634 ! contains covalently bound peptides at the N-termini of chains B, D, F and H
72970 ! contains covalently bound peptides at the N-termini of chains B and D
72957 ! contains covalently bound peptides at the N-termini of chains B and D
21638 ! contains covalently bound peptides at the N-termini of chains B and D
88630 ! probably orthologous to the mouse I-A group
100064 ! complexed with a hypocretin peptide
98766 ! complexed with deamidated gliadin peptide
63147 ! complexed with a human insulin peptide
88631 ! probably orthologous to the human HLA-DQ group
21640 ! contains covalently bound peptides
74111 ! contains covalently bound peptides at the N-termini of chains B, D, F and H
21644 ! contains covalently bound peptides
104297 !SQ Q69G19 27-263 # 95% sequence identity
21650 ! D2
21652 ! D2
62482 ! D2
21653 ! D2
21655 ! D2
79408 ! D2
21656 ! D2
94121 ! D4; putative family assignment as the region corresponding to C and C' strands is disordered
21657 ! D2
21658 ! domain 2
21659 ! domain 2
21660 ! domain 2
98199 ! domain 2
21662 ! domain 2
21661 ! domain 2
21663 ! domain 2
21664 ! domain 2
98206 ! domain 2
21665 ! domain 2
21666 ! domain 2
63162 ! domain 2
21670 ! domains 2 and 4
21674 ! domains 2 and 4
21678 ! domains 2 and 4
21679 ! domain 4
49157 ! a soluble form of b7-1
61973 ! complexed to ctla-4
21686 ! D1
21688 ! D1
62483 ! D1
21689 ! D1
21691 ! D1
79409 ! D1
21692 ! D1
94123 ! D3 and D5
21693 ! D1
49167 ! Rat and mouse sequences are identical for the two N-terminal modules
21701 ! modules 1 and 2
96611 ! modules 1, 2 and 3
21702 ! module 2
21703 ! module 1; from mouse protein
62312 ! module 3
104121 !SQ Q14896 358-451 # structure of a middle domain (641-770) is also known, 1gxe
65079 ! module I1
21709 ! module M5
21708 ! module M5
21710 ! module M5
21711 ! module M5
49175 ! different modules
49177 ! duplication: tandem repeat of 3 domains
49182 ! Duplication: tandem repeat of 4 domains, known as L1 domains
49184 ! tandem repeat of 4 L1 domains
21770 ! complex with VEGF
60970 ! swapped N-terminal strand dimer; only one subunit is in the PDB entry
21776 ! swapped N-terminal strand dimer
21777 ! swapped N-terminal strand dimer
21778 ! swapped N-terminal strand dimer
49196 ! possibly an intermediate structure between the I set and FnIII domains
106662 !SQ O75015 23-189
106648 !SQ O75015 23-189
49200 ! possibly an intermediate structure between the I set and FnIII domains
105035 !SQ P12319 29-196
89188 ! possibly an intermediate structure between the I set and FnIII domains
87484 ! complexed with IgA1 Fc
49202 ! possibly an intermediate structure between the I set and FnIII domains
49206 ! possibly an intermediate structure between the I set and FnIII domains
107829 !SQ Q8NHL6 25-218
107820 !SQ Q8NHL6 25-218
101519 ! possibly an intermediate structure between the I set and FnIII domains
69160 ! possibly an intermediate structure between the I set and FnIII domains
66482 ! a single-chain construct with epsilon chain domain, includes part of the linker
106111 !MQ P09693 P07766 # artificial chimera !SQ P09693 # CD3G_HUMAN T-cell surface glycoprotein CD3 gamma chain precursor 
69162 ! possibly an intermediate structure between the I set and FnIII domains
66483 ! a single-chain construct with gamma chain domain, includes part of the linker
106112 !MQ P09693 P07766 # artificial chimera !SQ P07766 # CD3E_HUMAN T-cell surface glycoprotein CD3 epsilon chain precursor
81296 ! "Early" Ig-like fold families possibly related to the immunoglobulin and/or fibronectin type III superfamilies
81279 ! subgroup of the larger IPT/TIG domain family
107645 !SQ P25799 245-350
107642 !SQ P25799 245-350
107635 !SQ P25799 245-350
107646 !SQ P25799 245-350
107651 !SQ P25799 245-350
107652 !SQ P25799 245-350
107305 !SQ Q9TYY1 195-660 
81282 ! domains of unknown function associated with different type of catalytic domains in a different sequential location ! subgroup of the larger IPT/TIG domain family
49209 ! follows the catalytic seven-bladed beta-propeller domain
106292 !SQ Q01745 42-680
69164 ! sequence identical to that of <i>Dactylium dendroides</i>
49237 ! follows the catalytic six-bladed beta-propeller domain
49231 ! precedes the catalytic alpha6/alpha6 domain
69167 ! precedes the catalytic incomplete alpha5/alpha5 barrel ! a rudiment form of Ig-like domain
49211 ! rudiment form of Ig-like domain; follows the catalytic (beta/alpha)8-barrel domain; family 20 glycosyl hydrolases
49215 ! follows the starch-binding domain C; the catalytic domain A has (beta/alpha)8-barrel fold; family 13 glycosyl hydrolases
108317 !SQ P05618
108333 !SQ P05618
108309 !SQ P05618
108325 !SQ P05618
81280 ! domain architecture similar to cyclomaltodextrin glycosylhydrolases
49221 ! precedes the catalytic (beta/alpha)8-barrel domain
81960 ! homologous to maltogenic amylase
101523 ! protein shares similar domain organization with maltogenic amylases but differs in the spatial arrangement of its domains
49226 ! elaborated with a few large insertions in the common fold ! precedes the catalytic (beta/alpha)8-barrel domain, the domain architecture similar to maltogenic amylases
49224 ! domain architecture similar to isoamylase
81962 ! domain architecture similar to isoamylase
49233 ! precedes the catalytic (beta/alpha)8-barrel domain
107427 !SQ P33136 23-511
89191 ! apart from the domains of transcription factors and sugar-utilizing enzymes
88380 ! complex with RalA
49228 ! elaborated with many loop insertions in the common fold
106892 !SQ P12823 281-675 # 99% sequence identity
106914 !SQ P12823 281-675 # 99% sequence identity
106898 !SQ P12823 281-675 # 99% sequence identity
94793 ! C-terminal domain only 
105311 !SQ Q8JU42 586-696
63668 ! similar to both C1 and C2 set
81287 ! implicated in lipid recognition, particularly in the recognition of pathogen related products
81964 ! a cholesterol binding protein
49256 ! contains additional N-terminal strand
21898 ! complex with rac (chain B)
61040 ! complex with rac1
72915 ! complexed with ARL2
72913 ! complexed with ARL2
72917 ! complexed with ARL2
81967 ! forms tetrameric cytoplasmic pore; contains a C-terminal extension
49235 ! elaborated with many loop insertions in the common fold
49236 ! Coagulation factor XIII
74844 ! GDP-binding protein
21896 ! Rod domains 5 and 6
21897 ! one repeat (Rod 4)
49244 ! duplication: contains tandem repeat of two elaborated Ig-like domains contacting each other head-to-head
49261 ! Arginine-specific cysteine proteinase ! follows the catalytic alpha/beta domains
69176 ! duplication: tandem repeat of two Ig-like domains
81295 ! truncated fold fused to an LRR domain
49267 ! tandem of fibronectin type III domains
103884 !SQ P13726 38-237
103845 !SQ P13726 33-242
107893 !SQ P13726 33-242
21975 ! repeats 7 through 10
21978 ! heparin and integrin binding segment
93665 ! first Fn3 module 
95663 ! anastellin, a fragment of the first Fn3 module
66439 ! ED-A domain
21979 ! ED-B domain
21989 ! tandem repeat of two Fn3 modules
21990 ! third Fn3 repeat
106784 !SQ Q05546 502-770
49276 ! tandem of fibronectin type III domains
84731 ! second Fn3 module
21996 ! first tandem pair of FnIII domains
49281 ! tandem of fibronectin type III domains
49289 ! duplication: consists of four similar domains; dimerizes by swapping the C-terminal strands of domains 1 and 3
22039 ! domain 4, the ligand-binding domain; complex with Fab
22040 ! domain 4, the ligand-binding domain
22053 ! 2nd domain
22054 ! 2nd domain
22059 ! N-terminal domain
61547 ! complexed with a cytokine
22070 ! 3rd N-terminal domain
74197 ! complexed with human cytomegalovirus IL-10
62706 ! complexed with IL-10
22071 ! module a71
99267 ! structural genomics; first Fn3 module
99468 ! structural genomics; second Fn3 module
99268 ! structural genomics; third Fn3 module
99285 ! structural genomics; first Fn3 module
108376 !SQ Q9P2J2 [Fragment] 634-728 # ! Structural genomics target
107766 !SQ P26992 202-305
104377 !SQ P00722
104357 !SQ P00722
49311 ! duplication
49312 ! Coagulation factor XIII,
74849 ! GDP-binding protein
22192 ! domain 1
22193 ! domain 1
22195 ! domain 1
22197 ! two-domain fragment
93397 ! prodomain
49317 ! synonym: uvomorulin
22201 ! two-domain fragment
22205 ! two-domain fragment
95598 ! two-domain fragment
22206 ! domain 1
81096 ! domain 1
74851 ! five-domain fragment
107610 !SQ Q62165 58-303
84113 ! apo form
61452 ! apo form
49329 ! has additional strand at N-terminus
22246 ! monomeric mutant
79794 ! thermostable mutant
22271 ! monomeric mutant
77441 ! monomeric copper-free mutant
22272 ! monomeric mutant
63152 ! complexed with Yccs copper chaperone
49338 ! Monomeric enzyme
104397 !SQ P96278
107165 !SQ Q01137
107169 !SQ Q01137
22300 ! second domain only
49344 ! has additional strand at N-terminus; the active site in a similar topological location as the Cu,Zn SOD site
61937 ! CASP4
107814 !SQ P48678 408-546  # ! Structural genomics target
49348 ! contains an additional N-terminal strand
49349 ! ear domain consists of two different subdomains
73220 ! complexed with eps15 dpf peptide (chain P)
73289 ! complexed with eps15 dpf peptide (chain P)
22315 ! CASP3
73218 ! complexed with epsin dpw peptide (chain P)
73194 ! complexed with epsin dpw peptide (chain P)
73196 ! complexed with amphiphysin fxdxf peptide (chain P)
74857 ! consist of a single subdomain
87078 ! complexed with the p56 binding peptide; chains P and Q
87780 ! complexed with rabaptin-5 peptide, chain B
49354 ! contains PP switch between strands D and C'
49356 ! consists of two domains of this fold; domain 2 has an additional strand at the C-terminus
22323 ! CA-atoms only
89208 ! 4L504 (ZC168.6) gene product
84747 ! structural genomics
101541 ! C55C2.2 gene product
101544 ! contains extra N-terminal sudbomain involved in dimerisation
49368 ! binds iron in the site that is topologically equivalent to the copper-binding site of cupredoxins
108969 !SQ Q46495 # 
108965 !SQ Q46495 # 
108961 !SQ Q46495 # 
84261 ! complexed with DsbC
98819 ! disulfide-linked complex with the C-terminal domain
49376 ! an enteropathogenic serotype
81987 ! contains two different domains of immunoglobulin-like fold
81988 ! a penicillin-binding protein with carboxypeptidase activity
101546 ! contains extra C-terminal strand
110070 ! dimeric in crystals; this dimer is a probable biological unit
107469 !SQ Q8EB92 # ! Structural genomics target
49379 ! sandwich; 9 strands in 2 sheet; greek-key; subclass of immunoglobin-like fold
49386 ! belongs to subfamily IIa
49388 ! belongs to subfamily IIb
22389 ! XBD1
59264 ! XBD1
60973 ! XBD2
59263 ! XBD1
22388 ! XBD1
60972 ! XBD2
49390 ! Pfam 00963
89209 ! endoglucanase 9G
22402 ! cohesin domain from scaffolding protein CipA
22403 ! cohesin-2 domain of cellulosome
22405 ! cohesin domain of cellulosome
93043 ! complexed with dockerin domain
104669 !SQ Q7WYN3 29-199
89210 ! duplication: contains two differently decorated domains of this fold
96799 ! complexed with fibrinopeptide B
49406 ! duplication: consists of two domains of this fold; C-terminal domain lacks the last strand
49408 ! similar to C-terminal domain of FimH
79780 ! N-terminal-deleted; bound to a peptide corresponding to the n-terminal extension of the papk pilus subunit, chains B and D
79749 ! N-terminal-deleted
108019 !SQ P24093 23-159 # 97% sequence identity to Afa-III adhesin (SQ Q57254 23-159)
108010 !SQ P24093 23-159 # 97% sequence identity to Afa-III adhesin (SQ Q57254 23-159)
108011 !SQ P24093 23-159 # 97% sequence identity to Afa-III adhesin (SQ Q57254 23-159)
108028 !SQ P24093 23-159 # 97% sequence identity to Afa-III adhesin (SQ Q57254 23-159)
106427 !SQ Q20646 223-418
22460 ! includes most of the linker with SH2 domain
49439 ! synonym: core binding factor alpha, cbfa
63684 ! almost identical sequence to the human protein
81993 ! common fold is decorated with many additional structures
79324 ! complex with DNA
107306 !SQ Q9TYY1 195-660 
49443 ! this domain is interrupted by a small domain which is barrel-sandwich hybrid fold
81999 ! includes the N-terminal tail
94508 ! complexed with a snare peptide
94498 ! complexed with a snare peptide
94503 ! complexed with a snare peptide
49447 ! duplication: one domain of this fold is inserted into another domain of the same fold
60974 ! complexed with P-selectin internalization peptide SHLGTYGVFTNAA
65680 ! complexed with ctla-4 internalization peptide ttgvyvkmppt
109243 !SQ Q9UM07
109240 !SQ Q9UM07
109237 !SQ Q9UM07
109528 !SQ Q9RT80 35-178
109500 !SQ Q9RT80 35-178
49451 ! sandwich; 7 strands in 2 sheets, greek-key ! variations: some members have additional 1-2 strands to common fold
103859 !SQ Q00019
49454 ! this domain is the last one in the protein chain
108318 !SQ P05618
108334 !SQ P05618
108310 !SQ P05618
108326 !SQ P05618
74035 ! complexed with Hif-1alpha oxyproline peptide (chain H)
74186 ! complexed with Hif-1alpha oxyproline peptide (chain D)
49474 ! sandwich; 8 strands in 2 sheets
104619 !SQ P02766 31-143
105847 !SQ P02766
105851 !SQ P02766
105801 !SQ Q9PTT3
105805 !SQ Q9PTT3
105797 !SQ Q9PTT3
49480 ! duplication: consists of two similar prealbumin-like domains
22628 ! a single b repeat unit (b1)
22632 ! two b repeat units (b1b2)
110094 ! the penultimate strand is in the other beta-sheet than in the Cna repeats
108814 !SQ P80564
106996 !SQ P80564
108790 !SQ P80564
106972 !SQ P80564
108766 !SQ P80564
106948 !SQ P80564
49483 ! sandwich; 9 strands in 2 sheets
49484 ! contains alpha-helical dimerization subdomain at the N-terminus
49486 ! alpha and beta chains are derived from a single-chain protomer and share this fold
110096 ! similar overall structure to Catechol 1,2-dioxygenase
105380 !SQ O67987
49492 ! sandwich; 6 strands in 2 sheets
49495 ! duplication: contains two domains of this fold
69188 ! sandwich; 6 strands in 2 sheets
110098 ! rudiment form of the PBP-5-like domain
107360 !SQ Q53613 21-383 # ! Structural genomics target
49497 ! sandwich; 6 strands in 2 sheets
81278 ! six-stranded beta-sandwich, jelly-roll/greek-key topology
81277 ! analogous to the Ig-like domain of arthropod hemocyanin; similar sequential but different spatial position relative the shared domain
49502 ! sandwich; 7 strands in 2 sheets, greek-key ! variations: some members have additional 1-2 strands
49503 ! contains copper-binding site
49504 ! mono-domain proteins
105481 !SQ P22364
105487 !SQ P22364
105470 !SQ P22364
105471 !SQ P22364
106454 !SQ P22364
22885 ! apo form
49527 ! basic blue protein
22917 ! Oxidized azurin II
22918 ! Reduced azurin II
23000 ! ruthenium-modified
23009 ! contains purple CuA centre introduced by loop-directed mutagenesis
63686 ! azurin-related protein
23022 ! CASP2
49551 ! consists of two domains of this fold
105828 !SQ P38501
105659 !SQ P38501
86892 ! atomic resolution structure
103904 !SQ O68601
23123 ! CA-atoms only
23117 ! CA-atoms only
103849 !SQ Q53239
103857 !SQ Q53239
103855 !SQ Q53239
108062 !SQ P07788
103923 !SQ P07788
103816 !SQ P07788
103937 !SQ P07788
103819 !SQ P07788
103822 !SQ P07788
49555 ! consists of three domains of this fold
49557 ! consists of three domains of this fold
108226 !SQ Q6H9H7 22-515
49559 ! consists of 6 domains of this fold
105434 !SQ Q28107 29-324,1566-2210
74874 ! eukaryotic signaling domain probably related to cupredoxins but lacking the metal-binding site
72456 ! complexed with ephb2
105562 !SQ O08543
110107 ! probably related to cupredoxins but lacking the metal-binding site 
109244 !SQ Q9UM07
109241 !SQ Q9UM07
109238 !SQ Q9UM07
74877 ! SS-crosslinked beta-sandwich of distinct geometry but topologically similar to cupredoxins
74879 ! duplication: tandem repeat of two homologous domains
110110 ! sandwich; 7 strands in 2 sheets, greek-key; permutation of the immunoglobulin-like fold
105865 !SQ Q92RG6
105842 !SQ Q92RG6
49561 ! sandwich; 8 strands in 2 sheets; greek-key
49562 ! two constituent families are related by circular permutation
49573 ! rudiment form lacking calcium-binding site
69196 ! Calcium-independent
49575 ! topologically similar to the C-terminal domain of PapD
49576 ! duplication: contains tandem repeat of two similar domains
107975 !SQ P21707 271-419
107974 !SQ P21707 271-419 
23192 ! first C2 domain ! CASP1
23193 ! first C2 domain
68212 ! second C2 domain
107047 !SQ P21707 271-419
109606 ! duplication: contains 2 C2 domains
23195 !SQ P40748 293-588
101562 ! duplication: contains 2 C2 domains
109041 !SQ P50232 288-425 # second C2 domain
109042 !SQ P50232 288-425 # second C2 domain
100262 ! first C2 domain
97467 ! first C2 domain
23205 ! CA-atoms only
89221 ! chaperone of F1 capsule antigen Caf1
49598 ! sandwich; 8 strands in 2 sheets; greek-key
49599 ! has a circularly permuted immunoglobulin-fold topology with extra strand
73389 ! complexed with a TANK peptide, chain B
73387 ! complexed with a TANK peptide, chain B
104915 !SQ Q13114 377-568
73798 ! complexed with a CD40 peptide, chain B
73797 ! complexed with a RANK peptide, chain B
49605 ! sandwich; 8 strands in 2 sheets; meander
49606 ! duplication: composed of two structural repeats
49608 ! can be classified as disulfide-rich
77130 ! Des 1-6 protein complexed with vasopressin
84174 ! Des 1-6 protein
82003 ! sandwich; 8 strands in 2 sheets; meander
82006 ! found only in some NusG species
82007 ! interrupted by an insert beta-sandwich domain
88632 ! sandwich; 8 strands in 2 sheets; jelly-roll; some members can have additional 1-2 strands ! characteristic interaction between the domains of this fold allows the formation of five-fold and pseudo six-fold assemblies
69203 ! oligomerizes into a pentameric ring structure
88634 ! the order of the chains N-VP0-VP3-VP1-C is as in the polyprotein; VP0 is cleaved later upon capsid assembly to VP4 and VP2 ! there is a different order in the shuffled genome of insect picorna-like proteins (Cricket paralysis virus)
23412 ! contains unprocessed VP0
72078 ! grafted HIV-1 v3 loop in chain B
49654 ! different genetic order of VP segments due to extensive genome shuffling
88636 ! duplication: mature coat protein consists of three similar domains that can be in a single chain or in two separate chains
49629 ! duplication: cnosists of three very similar domains
49627 ! chain 1 is one-domain VP23; chain 2 is two-domain VP37
63691 ! includes the P (protruding) domain of complex beta-structure containing a beta-barrel similar to the second domain of EF-TU
101569 ! contains an insert beta-sandwich domain
109148 !SQ P03608
49613 ! include capsid protein F and spike protein G
23278 ! chimera with a fragment 1-71 of vp1 from spiroplasma virus SPV4
105262 !SQ Q9JGS0 246-781
74888 ! a vector for human genome therapy
49749 ! duplication: consists of two domains of this fold packed together like the nucleoplasmin subunits ! trimeric; in the trimers, the domains are arranged around pseudo six-fold axis
82015 ! a large, lipid-containing, DNA virus
49753 ! each domain is heavily decorated with many insertions
49742 ! members of this superfamily bind peptide substrates ! duplication: consists of two domains of this fold packed together like the adjacent nucleoplasmin subunits
49694 ! sandwich; 8 strands in 2 sheets; greek-key ! duplication: has internal pseudo twofold symmetry
49697 ! duplication consists of two domains of this fold
23591 ! C-terminal domain only
23595 ! C-terminal domain only
23601 ! C-terminal domain only
65746 ! C-terminal domain only
49702 ! duplication consists of two domains of this fold
23619 ! circularly permuted sequence
23621 ! N-terminal domain only
49706 ! duplication consists of two domains of this fold
23622 ! N-terminal domain
63693 ! shares putative chitin-binding site with SKLP
60517 ! CASP4
49722 ! sandwich; 8 strands in 2 sheets; complex topology ! duplication: has weak internal pseudo twofold symmetry
49736 ! pancreatic lipase related protein 1
49737 ! pancreatic lipase related protein 2
49757 ! sandwich; 8 strands in 2 sheets; jelly-roll
96549 ! mu-like isoform with the large and small subunits fused in a single chain
101575 ! sandwich; 8 strands in 2 sheets; jelly-roll; similarity to the Nucleoplasmin-like/VP fold
104015 !SQ O76054
89231 ! sandwich; 8 strands in 2 sheets; jelly-roll
85552 ! structural genomics
63696 ! sandwich; 8 strands in 2 sheets; jelly-roll
59629 ! CASP4
49763 ! sandwich; 8 strands in 2 sheets; greek-key
101580 ! Pfam 04969
100919 ! beta-sandwich: 8 strands in 2 sheets
90346 ! complexed with peptide, chain B
90340 ! complexed with peptide, chain B
95900 ! complexed with peptide nrllltg, chain B
49771 ! sandwich; 8 strands in 2 sheets; complex topology with the crossing loops
62349 ! a monomeric form
49776 ! sandwich; 8 strands in 2 sheets; greek-key: partial topological similarity to immunoglobulin-like folds
23703 ! CASP3
100730 ! structural genomics 
63706 ! sandwich; 8 strands in 2 sheets; greek-key: partial topological similarity to immunoglobulin-like folds
104312 !SQ P17900 31-193
104313 !SQ P17900 31-193
63711 ! sandwich; 8 strands in 2 sheets; greek-key: partial topological similarity to immunoglobulin-like folds
49784 ! sandwich; 9 strands in 2 sheets; jelly-roll
106293 !SQ Q01745 42-680
69209 ! sequence identical to that of <i>Dactylium dendroides</i>
105436 !SQ Q28107 29-324,1566-2210
105563 !SQ P54763 27-207
72452 ! complexed with ephrin b2
104378 !SQ P00722
104358 !SQ P00722
76350 ! complex with cellopentaose
23769 ! first N-terminal CBD
23768 ! first N-terminal CBD ! CASP2
23770 ! second N-terminal CBD
72039 ! second CBM4
72032 ! second CBM4
100171 ! CBM6-2
100211 ! CBM6-2; complexed with cellobiose
100213 ! CBM6-2; complexed with cellotriose
100215 ! CBM6-2; complexed with xylotetraose
100173 ! CBM6-2; complexed with glc-1,3-glc-1,4-glc-1,3-glc
100216 ! CBM6-2; complexed with glc-4glc-3glc-4glc
86825 ! CBM6-3, in complex with laminaribiose
86678 ! CBM6-3, in complex with cellobiose
108131 !SQ P33558 243-374 # CBM6-2, the structure of the C-terminal domain, CBM6-3 (384-512) is also known
108129 !SQ P33558 243-374 # CBM6-2, the structure of the C-terminal domain, CBM6-3 (384-512) is also known
108128 !SQ P33558 243-374 # CBM6-2, the structure of the C-terminal domain, CBM6-3 (384-512) is also known
108130 !SQ P33558 243-374 # CBM6-2, the structure of the C-terminal domain, CBM6-3 (384-512) is also known
85486 ! third CBM6 module, CBM6-3, in complex with xylotriose
86668 ! CBM6-3, unbound
69218 ! synonym: Pseudomonas cellulosa
66431 ! CASP4
49811 ! CBM family 22, formerly x6b domain
104193 !SQ P77847 36-220
104194 !SQ P77847 36-220
83348 ! the second CBM29
83347 ! the second CBM29
103939 !SQ Q9C171 337-477
83346 ! the second CBM29
49815 ! the single-strand break repair protein
101589 ! duplication: tandem repeat of two similar domains
101590 ! Yir029w
92496 ! structural genomics
82022 ! a truncated form of this fold lacking one of the N-terminal strands
89249 ! a truncated form of this fold lacking one of the N-terminal strands
109408 !SQ Q93UV9 207-640
109410 !SQ Q93UV9 207-640
109412 !SQ Q93UV9 207-640
108080 !SQ P06564 578-761
109419 !SQ P71140 34-228 # chain B coverage
103860 !SQ Q00019
49817 ! sandwich; 9 strands in 2 sheets; jelly-roll; form trimers
49818 ! forms homotrimers
49819 ! this domain is inserted into a multihelical domain
49824 ! includes rudiment esterase domain
97947 ! 1934 human H1
97899 ! 1930 swine H1
97935 ! 1930 swine H1
97887 ! 1930 swine H1
97959 ! 1934 human H1
97847 ! 1934 human H1
97312 ! 1918 human H1
97893 ! 1918 human H1
49827 ! includes irregular N- and C-terminal extensions
82025 ! sandwich; 9 strands in 2 sheets; greek-key
101595 ! sandwich; 9 strands in 2 sheets; greek-key
101600 ! sandwich; 9 strands in 2 sheets; greek-key/jelly-roll
101603 ! similar to calpain-like protein fragment from Trypanosoma brucei and the L2230.07 gene product from Leishmania major 
97189 ! structural genomics
101605 ! sandwich; 9 strands in 2 sheets; jelly-roll
49829 ! sandwich; 9 strands in 2 sheets; greek-key; contains a few helices in loop regions
110131 ! sandwich; 9 strands in 2 sheets; unusual topology with 2 crossover loops
108037 !SQ P23065 8-160
49834 ! sandwich, 10 strands in 2 sheets; greek-key
108093 !SQ Q64823 181-365 
108096 !SQ Q64823 181-365 
108099 !SQ Q64823 182-365
49841 ! sandwich, 10 strands in 2 sheets; jelly-roll
69229 ! also includes the PDB entry </i>(<a href="../pdb.cgi?pdb=1otz">1otz</a>)<i> that together with the entry </i>(<a href="../pdb.cgi?pdb=1p0t">1p0t</a>)<i> provides the multimeric structure of the complex of this protein with its receptor, BAFF-R. In these entries protein chains are designated by both upper case and lower case letters creating problems with its processing and presentation in SCOP
87386 ! complexed with a br3 derived peptide; chains G, H, I, J, K and L
101613 ! hetrotrimer of A, B and C chains
101615 ! hetrotrimer of A, B and C chains
101617 ! hetrotrimer of A, B and C chains
49853 ! sandwich, 10 strands in 2 sheets; jelly-roll
89256 ! duplication: contains two CUB domains separated by an EGF-like domain
106147 !SQ O00187 17-181
89260 ! N-terminal strand appears only in calcium-free form
49862 ! sandwich, 10 strands in 2 sheets; "folded meander"
109169 !SQ Q54873 287-1007
89266 ! domain 4
63723 ! sandwich, 10 strands in 2 sheets;
63724 ! some topological similarity to osmotin
107522 !SQ P61914 40-214
49869 ! sandwich; 11 strands in 2 sheets
49870 ! has two smaller insertion domains
101620 ! antifungal protein
49874 ! antifungal protein
104216 !SQ P02883
23906 ! CA-atoms only ! structure in this entry is partly incorrect, correction published
49878 ! sandwich; 11 strands in 2 sheets; greek-key
49879 ! has a few short helices inserted in loops
79419 ! complex with Ski
107721 !SQ Q13485 314-546
107730 !SQ Q13485 314-546
107722 !SQ P84022 228-425
107731 !SQ P84022 228-425
23917 ! complexed with a phosphothreonine peptide
68119 ! complex with a rad9-derived phosphothreonine peptide
66388 ! complex with a rad9-derived phosphothreonine peptide
66384 ! complexed with a phosphothreonine peptide
66387 ! complex with a rad9-derived phosphothreonine peptide
66383 ! complexed with a phosphotyrosyl peptide
68060 ! complexed with a phosphothreonine peptide
68118 ! complex with a rad9-derived phosphothreonine peptide
68059 ! complexed with a phosphotyrosyl peptide
23920 ! complexed with a phosphotyrosyl peptide
70690 ! complexed with a synthetic phosphopeptide
99401 ! structural genomics
101630 ! weak sequence similarity to SMAD domain
49888 ! sandwich; 11 strands in 2 sheets; greek-key
49893 ! sandwich; 14 strands in 2 sheets; greek-key
49894 ! has a few helices inserted in loops
49896 ! Apoptotic caspase inhibitor
66023 ! after caspase cleavage
61685 ! complexed to caspase-8
66020 ! after caspase cleavage
49898 ! sandwich; 12-14 strands in 2 sheets; complex topology
49901 ! natural circle permutation: the "old" N- and C-termini are linked with a peptide bond, whereas the "new" ones correspond to a cleaved loop
23962 ! demetallized, pH 5
61592 ! complexed with dimannose
63309 ! complexed with a hexapeptide
90659 ! complexed with a tripeptide ypy, chain B
23988 ! Zinc-calcium substituted
71891 ! complexed with a 10-mer peptide
77215 ! complexed with a carbohydrate-mimicking 12-mer peptide
66997 ! complexed with a hexapeptide
77211 ! complexed with a carbohydrate-mimicking 15-mer peptide
49905 ! two-chain protein resulted from a single-chain precursor
49906 ! two-chain protein resulted from a single-chain precursor
105512 !SQ P16404
108193 !SQ Q6YD91
108185 !SQ Q6YD91
108189 !SQ Q6YD91
49914 ! a legume lectin that delays hematopoietic progenitor maturation
24132 ! Db58
49916 ! natural circle permutation resulting from a post-translational modification of precursor
63729 ! natural circle permutation resulting from a post-translational modification of precursor
101633 ! natural circle permutation resulting from a post-translational modification of precursor
49920 ! single-chain subunit has "generic" topology
74904 ! mammalian protein related to legume lectins
24175 ! circularly permuted
24177 ! circularly permuted
24178 ! circularly permuted
24180 ! circularly permuted
24182 ! interrupted by the insertion of a xylanase domain from <i>Bacillus subtilis</i>
89270 ! a natural circularly permuted protein
49930 ! 1,3-alpha-1,4-beta-D-galactose-4-sulfate-3,6-anhydro-D-galactose 4 galactohydrolase
49936 ! galectin-1 homologue CG-16
93268 ! lg4-5 domain pair
24224 ! lg4-5 domain pair
24228 ! fifth G-like module
101641 ! alternative splicing
101643 ! Pfam 05735
24251 ! complexed with phosphocholine
73938 ! calcium-depleted
72886 ! in complex with 2-O-methyl-alpha-D-N-acetyl neuraminic acid
93411 ! structural genomics; MCSG target APC1120
101649 ! members have same function and similar structures but low sequence similarity
108473 !SQ Q9I4H0 # ! Structural genomics target
107761 !SQ Q9RB42
49966 ! both domains have this fold ! rest of protein is beta-propeller of six sheets
109039 !SQ P37060
109036 !SQ P37060
105150 !SQ Q26966
105146 !SQ Q26966
105148 !SQ Q26966
49971 ! contains many insertions in the common fold
24291 ! CASP2
101652 ! flat sheet beta-sandwich lacking the characteristic beta-bulge in the C-terminal strand
49979 ! Partial overlap with common fold and the active sites of the other endoglucanases
24316 ! inserted into a beta-glucanase domain from <i>Bacillus macerans</i>
106570 !SQ P55328 29-210 # 100% sequence identity; Aspergillus awamori TaxID: 105351
89272 ! endoxylanase 11a
106791 !SQ Q9HFH0
108044 !SQ Q8NJY3 31-254
109129 !SQ Q8NJY3 31-254
108042 !SQ Q8NJY3 31-254
108043 !SQ Q8NJY3 31-254
101656 ! circular permutation of the canonical fold
109233 !SQ Q8NK89 19-499
109235 !SQ Q8NK89 19-499
49993 ! sandwich; 18 strands in 2 sheets
74650 ! probable carbohydrate-binding domain in enzymes acting on sugars
89278 ! 5C981 (C01B4.6 or YK2391) gene product
84718 ! structural genomics; NESG target WR66
84192 ! structural genomics
104379 !SQ P00722
104359 !SQ P00722
109170 !SQ Q54873 287-1007
89284 ! domain 3
63733 ! overall domain organization is similar to Bacterial glucoamylase
108412 !SQ Q76IQ9
108410 !SQ Q76IQ9
108414 !SQ Q76IQ9
82042 ! overall domain organization is similar to Lactobacillus maltose phosphorylase
89286 ! family 57 glycoside hydrolase; overall domain organization is similar to that of the alpha-mannosidase family
88656 ! family 38 glycoside hydrolase; overall domain organization is similar to that of the 4-alpha-glucanotransferase family ! the supersandwich domain is elaborated with additional beta-strands and beta-sandwich subdomains
89289 ! the single-chain precursor is processed into 5 peptides; heavily glycosylated
110148 ! Pfam coverage extends to the C-terminal immunoglobulin-like domain
107428 !SQ P33136 23-511
103861 !SQ Q00019
105578 !SQ P46881 9-628
105575 !SQ P46881 9-628
63736 ! duplication: two beta-sandwiches of similar topologies are fused together in a single three beta-sheet domain
105942 !SQ P09960 
50011 ! consists of two beta-sandwich domains of similar topologies
83462 ! N-terminal domain in complex with RNA
83464 ! N-terminal domain in complex with RNA
82045 ! consists of two different beta-sandwich domains of partial topological similarity to immunoglobulin-like folds
50016 ! consists of two different beta-sandwich domains unrelated to other beta-sandwich folds
50019 ! the trigger of tail contraction and the long tail fibers connector
98381 ! alternative fit of the first 19 residues
50021 ! consists of two all-beta subdomains: conserved small domain has a rubredoxin-like fold; larger domain consists of 6 beta-stands packed in either sandwich of two 3-stranded sheets or closed barrel (n=6; S=8)
104275 !SQ P13272 # precursor of chains I,E and V,R
104245 !SQ P13272 # precursor of chains I,E and V,R
105898 !SQ P13272 79-274
108886 !SQ Q00458
105647 !SQ Q00458
107927 !SQ Q53122 17-451
107936 !SQ Q53122 17-451
82050 ! this fold is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich ! these regions form six left-handed collagen-like helices packed and H-bonded together
101668 ! TT1381
50036 ! barrel, partly opened; n*=4, S*=8; meander ! the last strand is interrupted by a turn of 3-10 helix
50037 ! the N-terminal domains of these repressors bind DNA
104087 !SQ P33120
91175 ! a circular form
91174 ! a circular form
91173 ! a circular form
84749 ! complex with Sap SH2 domain bound to slam peptide, chain B
80425 ! N-and C-terminal labeled protein
78770 ! Solid-state MAS NMR structure
24488 ! circular permutant
24489 ! circular permutant
24492 ! circular permutant
66610 ! complexed with peptide
50067 ! v-src
60435 ! C-terminal domain
24536 ! N-terminal domain
24535 ! C-terminal domain
24537 ! C-terminal domain
24538 ! C-terminal domain
24540 ! N-terminal domain
24541 ! N-terminal domain
24539 ! N-terminal domain
24542 ! N-terminal domain
24543 ! N-terminal domain
50073 ! Sex muscle abnormal protein 5
24545 ! C-terminal domain
24547 ! C-terminal domain
24549 ! C-terminal domain
84343 ! C-terminal domain
84391 ! C-terminal domain
99962 ! C-terminal domain; complexed with a mitogen-activated protein kinase kinase peptide, chain D
86910 ! C-terminal domain; complexed with a peptide from the lymphocyte cytosolic protein 2, chains C and D
83468 ! C-terminal domain; complexed with an RxxK-containing slp-76 peptide, chain B
50080 ! synonyms: Myc box dependent interacting protein 1, bin1
91467 ! complexed with c-Myc peptide, chain A
91468 ! the remaining residues, 270-401 are not ordered apart a short bound segment 303-312
61478 ! segment-swapped dimer
24556 ! segment-swapped dimer
60436 ! complexed to Grb2 SH3 domains
69248 ! associates with a guanylate kinase domain
85661 ! N-terminal domain forms a segment-swapped dimer; C-terminal domain includes the autoinhibition tail region, residues 284-333
88482 ! N-terminal domain forms a segment-swapped dimer; C-terminal domain includes the autoinhibition tail region, residues 284-336
87454 ! N-terminal domain forms a segment-swapped dimer; C-terminal domain binds a peptide from p22phox, chains C and D
72065 ! C-terminal SH3 domain complexed with the C-terminal tail of p47phox (chain P)
80065 ! complexed with a peptide of pex14p, chains P and Q
107848 !SQ Q9NZM3 982-1037 # there are structures for other SH3 domains (761-841; 897-957; 1055-1121; 1102-1186) ! third SH3 domain
103839 !SQ Q9NZM3 897-957 # ! second SH3 domain
99335 ! structural genomics; first SH3 domain
99212 ! structural genomics; fifth SH3 domain
99255 ! structural genomics; fourth SH3 domain
99397 ! structural genomics; C-terminal SH3 domain
99360 ! structural genomics; second last SH3 domain
99367 ! structural genomics
99449 ! complexed with a ubpy-derived peptide
93386 ! structural genomics; C-terminal domain
97506 ! helically extended ant the N-terminus
106207 !SQ P54288 96-191
106211 !SQ P54288 96-191
106358 !SQ P54288
106379 !SQ P54288
108916 !SQ P54287 38-362
108910 !SQ P54287 38-362
108920 !SQ P54287 38-362 # beta4 isoform with odd numbering
105877 !SQ Q9DBJ3 343-401 # ! Structural genomics target
82059 ! duplication: tandem repeat of three SH3-like GW domains
105953 !SQ P24733 6-837
105263 !SQ P24733 3-836
63749 ! Pfam 00567
110163 ! duplication; contains two Tudor domains in tandem
105983 !SQ Q12888 1484-1606
69250 ! includes the C-terminal all-alpha subdomain
89299 ! contains extended 'arm', N-terminal to the common fold core
89300 ! duplication: contains tandem repeat of two MBT repeats
54160 ! SH3-like barrel is capped by a C-terminal helix
109230 !SQ P13123
109231 !SQ P13123
54165 ! lacks the SH3-like barrel first strand that can be complemented by bound peptide ligand; in shadow chromo domain the corresponding site is altered by insertion; similarity to the IL8-like fold
54166 ! duplication: consists of two homologous domains, N-terminal chromo domain and C-terminal chromo shadow domain
37474 ! C-terminal shadow chromo domain
70584 ! Chromo domain complexed with the lysine 9-methyl histone H3 N-terminal peptide
37475 ! N-terminal chromo domain
98516 ! Chromo shadow domain complexed with pxvxl motif peptide of caf-1, chain C
72771 ! Chromo domain complexed with histone h3 tail containing dimethyllysine 9
72774 ! Chromo domain complexed with histone h3 tail containing trimethyllysine 9
37477 ! C-terminal shadow chromo domain
94655 ! complexed with histone H3 peptide containing trimethyllysine 27, chain B
94590 ! complexed with histone H3 peptide containing trimethyllysine 27, chain B
106287 !SQ Q9VUQ5 602-720
106286 !SQ Q9VUQ5 602-720
108904 !SQ Q9VUQ5 602-717
97173 ! fused with MBP
105569 !SQ Q9UL18 225-349 ! complex with a siRNA-like duplex
105570 !SQ Q9UL18 225-349 ! complex with a siRNA-like duplex
110167 ! includes the N-terminal domain
107539 !SQ Q8U3D2 # consists of 4 domains: N-terminal (1-152,269-323) [two ferredoxin-like folds inserted one in the other]; PAZ (153-268); middle (324-547) [alpha/beta, 3layers a/b/a; parallel 4-stranded beta-sheet, order 2134]; PIWI (548-770)
107179 !SQ Q20728 132-229 # ! Structural genomics target
74173 ! structural genomics
50101 ! contains irregular array of helices in the N-terminal extension
50103 ! also <i>Rhodococcus sp.</i> R312
107832 !SQ Q7SID3
107836 !SQ Q7SID3
107838 !SQ Q7SID3
107834 !SQ Q7SID3
50104 ! many known members contain KOW motif
105339 !SQ P10972
105336 !SQ P12734
24609 ! CASP3
109493 !SQ Q9N9V6 # ! Structural genomics target
107785 !SQ Q76G20 # RL to eIF5a: 1-126 
105318 !SQ P20276
24612 ! CA-atoms only; includes the C-terminal tail
92364 ! C-terminal domain (Ngc) only
50118 ! contains insert beta-sheet subdomain and C-terminal helix
50120 ! topoisomerase poison
88400 ! complexed with the antidote protein MazE
63434 ! contains 5 short helices in the loop between the third and fourth strands
101697 ! contains extra N-terminal all-alpha subdomain
98831 ! structural genomics
50128 ! contains barrel, partly opened; n*=4, S*=8; meander
24655 ! CA-atoms only
109336 !SQ P61492
109388 !SQ P61492
50136 ! C-terminal domain is alpha/beta (classical Rossmann-fold)
50137 ! contains a Zn-finger subdomain, residues 94-117
24664 ! steroid-active isozyme
74531 ! glutathione-dependent formaldehyde dehydrogenase
74570 ! glutathione-dependent formaldehyde dehydrogenase
24710 ! gamma-2 isozyme
79372 ! glutathione-dependent formaldehyde dehydrogenase
24712 ! beta-1 isozyme
74607 ! glutathione-dependent formaldehyde dehydrogenase
24722 ! sigma isozyme
84931 ! glutathione-dependent formaldehyde dehydrogenase
24730 ! sigma isozyme
24734 ! glutathione-dependent formaldehyde dehydrogenase
24732 ! alpha isozyme
24740 ! sigma isozyme
100792 ! structural genomics
92644 ! structural genomics
103898 !SQ P26646 # ! Structural genomics target
24765 ! CASP4
100794 ! structural genomics
104477 !SQ Q04894
104158 !SQ Q04894
104302 !SQ Q04894
108343 !SQ Q9EQZ5
108347 !SQ Q9EQZ5
108339 !SQ Q9EQZ5
73451 ! in complex with the RNA target
50155 ! contains barrel, partly opened; n*=4, S*=8; meander; capped by alpha-helix
50156 ! peptide-binding domain
50157 ! Pfam 00595
24771 ! third PDZ domain
99579 ! third PDZ domain
50162 ! Synonym: synapse associated protein 90, sap90 ! duplication: contains three PDZ domains
24774 ! third PDZ domain
24775 ! third PDZ domain
83707 ! first PDZ domain
24776 ! second PDZ domain
83708 ! first PDZ domain
104931 !SQ P31016 62-154
72369 ! first PDZ domain
97151 ! second PDZ domain
86163 ! second PDZ domain
86783 ! second PDZ domain; complexed with an interleukin 5 receptor alpha peptide, chain B
86789 ! tandem of two PDZ domains; complexed with an interleukin 5 receptor alpha peptide, chain P
86785 ! second PDZ domain; complexed with an interleukin 5 receptor alpha peptide, chains P and Q
85462 ! tandem of two PDZ domains
84536 ! complexed with a peptide from Daper 1, chains D, E and F
70080 ! PDZ2 domain
24782 ! PDZ2 domain
96059 ! alternatively spliced PDZ2 domain
93845 ! alternatively spliced PDZ2 domain
70271 ! PDZ2 domain
60400 ! first PDZ domain
61990 ! first PDZ domain
70340 ! first PDZ domain
76274 ! first PDZ domain
62383 ! first PDZ domain; complexed with a Norpa C-terminal peptide
78676 ! seventh PDZ domain
93898 ! first PDZ domain
93897 ! first and second PDZ domains
108383 !SQ Q925T6 461-570 # ! Structural genomics target
79043 ! complexed with the carboxy-terminal tail of the erbb2 receptor
79044 ! complexed with the carboxy-terminal tail of the erbb2 receptor
80275 ! complexed with a phage-derived peptide
101716 ! Cg5884-pa
98236 ! complexed with peptide, chain B
91691 ! sixth PDZ domain
91693 ! sixth PDZ domain; complexed with liprin C-terminal peptide, chains C and D
99270 ! structural genomics; third PDZ domain
99271 ! structural genomics; first PDZ domain
99281 ! structural genomics; fourth PDZ domain
99470 ! structural genomics; second PDZ domain
99286 ! structural genomics; first PDZ domain
99288 ! structural genomics; second PDZ domain
99359 ! structural genomics; third PDZ domain
99400 ! structural genomics; Rsgi Ruh-005 domain
99433 ! structural genomics; Rsgi Ruh-006 domain
99454 ! structural genomics; Rsgi Ruh-003 domain
99578 ! structural genomics; Rsgi Ruh-007 domain
99469 ! structural genomics; fourth PDZ domain
101733 ! SH3 and multiple ankyrin repeat domains protein 1 
108378 !SQ O70209 4-93 # ! Structural genomics target
108390 !SQ Q9C0E4 238-341 # ! Structural genomics target
108394 !SQ Q9ES64 741-850 # ! Structural genomics target
108466 !SQ Q8BWR8 506-603 # ! Structural genomics target
108474 !SQ Q8R1G6 3-83 # ! Structural genomics target
74934 ! duplication: tandem repeat of two PDZ domains
105856 !SQ P31137 
105863 !SQ P31137 
108514 !SQ P31137 
50175 ! core: barrel, in some members open; n*=4, S*=8; meander
50178 ! duplication: the two domains share a common fold
24795 ! CASP2
50181 ! core: barrel, open; n*=4, S*=8; meander; SH3-like topology
50183 ! forms homo and heteroheptameric ring structures
24803 ! CASP3
24809 ! CASP3
63759 ! MTH649, smap1
84149 ! structural genomics
63760 ! smap1
61804 ! complexed with short poly-U RNA
78827 ! complexed with a uridine heptamer
89317 ! contains additional C-terminal alpha+beta domain
74939 ! forms homohexameric ring structures
82091 ! forms homoheptameric ring structure very similar to those of the archaeal and eukaryotic Sm proteins
71168 ! structural genomics
101737 ! core: barrel, open; n*=4, S*=8; meander; SH3-like topology; some similarity to the Sm-like fold
101740 ! a specificity-enhancing factor for the ClpXP proteolytic machine
93680 ! complexed with a SsrA peptide; chains I, J, K, L, M, N, O and P
93544 ! complexed with a SsrA peptide; chains C and D
101743 ! core: barrel, open; n*=4, S*=8; meander; SH3-like topology; some similarity to the Sm-like fold
101745 ! two available NMR structures display similar topologies but different barrel shapes
101750 ! core: barrel, closed; n=4, S=8; complex topology; helix-containing crossover connection
101752 ! a self-assembling amphiphile
50192 ! barrel, closed; n=5, S=8, meander
24810 ! CASP1
105330 !SQ P22450
50198 ! barrel, closed or partly opened n=5, S=10 or S=8; greek-key
50200 ! barrel, closed; n=5, S=10
107287 !SQ P00644
83192 ! thermonuclease, thermostable engineered enzyme
107239 !SQ P00644
107285 !SQ P00644
24864 ! OB-fold subdomain only
24846 ! swapping segment dimer of a deletion mutant
24959 ! extended C-terminally with a peptide with anti-hsv activity
24964 ! extended C-terminally with a peptide with anti-hsv activity
50208 ! barrel, partly opened; n*=5, S*=10
50210 ! phage-borne toxin; bacteriophages H30 and H19B
25059 ! complex with Gb3 trisaccharide
25054 ! A mutant shiga-like toxin IIe
50212 ! identical sequence with verotoxin-1 B
50213 ! N-terminal domain in S2/S3 has C-lectin-like fold
59140 ! mutant vaccine
105652 !SQ P23313
105644 !SQ P23313
106493 !SQ P23313
108056 !SQ P08095
108266 !SQ Q9ZFS5 36-231
108270 !SQ Q9ZFS5 36-231
107444 !SQ Q7BAE3
107450 !SQ Q7BAE3
50243 ! contains an irregular alpha+beta subdomain in the C-terminal extension
70704 ! complexed with proMMP-2
104383 !SQ Q90685 # ! Fragment
101757 ! Pfam 04076, Domain of unknown function DUF388
92013 ! structural genomics
50250 ! barrel, closed; n=5, S=10
50251 ! this is N-terminal domain in prokaryotic enzymes and the first "visible" domain in eukaryotic enzymes
89323 ! non-discriminating and archaeal-type enzyme
50259 ! barrel, closed; n=5, S=10
50260 ! tetramer; binds Holliday junction
50263 ! barrel, closed; n=5, S=10
105248 !SQ Q04837
90464 ! complexed with ssDNA
105974 !SQ P02339 
105448 !SQ Q9RY51 
89324 ! similar to the domains of the Replication protein A
50267 ! duplication: consists of three domains of this fold; contains zinc-finger insert in the C-terminal domain, residues 479-511
25299 ! the N-terminal two domains free
25301 ! the N-terminal two domains in complex with ssDNA
73483 ! C-terminal domain only
25302 ! N-terminal domain only
50273 ! duplication: consists of three domains of this fold
68300 ! two-domain fragment
82099 ! duplication: tandem repeat of three OB-fold domains
79197 ! complex with ssDNA
50280 ! domain of the p43 protein
25315 ! contains C-terminal His tag
25318 ! contains C-terminal His tag
89326 ! EMAP II-like domain found in vertebrata and insect enzymes; free domain possesses a cytokine activity
89329 ! YgjH
101763 ! aq_422; putative methionyl-tRNA synthetase beta subunit
63770 ! possesses export-related chaperone and tRNA-binding activities
50282 ! barrel, closed; n=5, S=8
25327 ! CASP2
25328 ! partly disordered
63772 ! evolutionary link between IF1 and eIF1a
74950 ! includes an all-alpha subdomain in the C-terminal extension
104556 !SQ P05198 
25341 ! CASP3
109494 !SQ Q9N9V6 # ! Structural genomics target
50299 ! incomplete OB-fold lacking the last strand
50301 ! includes the N-terminal tail
105319 !SQ P20276
25344 ! CA-atoms only
25357 ! low-resolution NMR-structure
101765 ! incomplete OB-fold lacking the last strand
92316 ! structural genomics; NESG target JR19
91828 ! structural genomics
110196 ! duplication: contains two domains of this fold
107787 !SQ Q76G20 # RL to eIF5a: 1-126 
105773 !SQ P21513 35-125
105808 !SQ P21513 35-125
105718 !SQ P21513 35-125
107555 !SQ Q9X242 # TM1717
101768 ! Pfam 01938
87663 ! complexed with the phosphorylated carboxyl-terminal peptide of RNA polymerase II, chains C and D
50315 ! barrel, open; n*=5, S*=8; the members' structures vary greater that those from cellular organisms
25386 ! incorrect structure
50319 ! contains a Zn-finger subdomain, res. 63-111
89333 ! MCM complex protein; dodecamer assembly; includes the N-terminal all-alpha subdomain and inserted Zn-finger
50321 ! duplication; contains tandem repeat of two incomplete OB-folds; forms a single barrel; n=8, S=10
25394 ! CA-atoms only
50325 ! barrel, closed; n=5, S=8
50326 ! eukaryotic enzyme has additional secondary structures at both N- and C-termini
50333 ! homohexamer: trimer of the C-terminal strand swapped dimers
50335 ! duplication: tandem repeat of two OB-fold domains with swapped C-terminal strands
81158 ! molybdate-activated form
50338 ! probably stems out from the biMOP domain
58984 ! CASP4
50342 ! duplication: tandem repeat of two swapped domains, one with a canonical OB-fold topology and one with a circular permutation
50345 ! core: barrel, partly opened; n*=5, S*=8; meander
101773 ! homodimeric protein; subunits are composed of a stand-alone copy of this domain 
94890 ! structural genomics
107961 !SQ P11846
110202 ! contains an N-terminal alpha-haipin and other fold decorations 
107826 !SQ Q80VC9 1112-1240 # ! Structural genomics target
50352 ! barrel, closed; n=6, S=12; and a hairpin triplet; meander ! duplication: has internal pseudo threefold symmetry
25489 ! 154 residue form
25520 ! Heparin-linked biologically-active dimer
25526 ! heparin-linked biologically-active dimer
104403 !SQ P05230
104399 !SQ P05230
104401 !SQ P05230
25534 ! Rat FGF7 + human FGF1 chimera
25555 ! CA-atoms only
25558 ! CA-atoms only
25560 ! CA-atoms only
106710 !SQ O61793 # ! Structural genomics target
50372 ! duplication: consists of two domains of this fold
83287 ! X-ray derived abrin-based sequence
50375 ! different sequence variants
104319 !SQ P81446 269-531 # 91% sequence identity
104316 !SQ P81446 269-531 # 91% sequence identity
106857 !SQ Q6ITZ3 266-520
104106 !SQ Q6ITZ3 266-520
105948 !SQ O06522 57-223
105950 !SQ O06524 25-178 
108502 !SQ Q868M7 11-442
50382 ! this superfamily is distinct from the ricin B-like lectin superfamily
50384 ! duplication: the tandem repeat of beta-trefoil domains
104851 !SQ P83667
104852 !SQ P84144,P84145 # two chains probably resulted from a single chain precursor
50399 ! overall fold is very similar to that of the STI family
50407 ! duplication: tandem repeat of four domains
110217 ! contains rudiment hairpin triplet lacking one hairpin
107307 !SQ Q9TYY1 195-660 
109234 !SQ Q8NK89 19-499
109236 !SQ Q8NK89 19-499
50412 ! barrel, closed; n=6, S=10; greek-key
63783 ! duplication: consists of two homologous domains
63784 ! trimerizes via the additional C-terminal helix
104169 !SQ P29015 1-87
61435 ! N-terminal domain only
61521 ! N-terminal domain only
63381 ! coupled with a NADP-binding domain of alpha/beta class
25658 ! CASP3
104626 !SQ P20070 33-300
50430 ! contains additional 2Fe-2S ferredoxin domain
72894 ! contains 2Fe-2S cluster in the C-terminal extension
50436 ! contains additional globin domain
50438 ! there is an alpha-helical subdomain inserted in this domain
107131 !SQ P29476 750-1413
89338 ! encoded by FLJ11149
101787 ! TM0379
106602 !SQ Q9WZW1  
106610 !SQ Q9WZW1  
106606 !SQ Q9WZW1  
25679 ! CASP2
50449 ! N-terminal domain is related to G proteins; C-terminal domain is (6,10) barrel of circularly permuted topology
103900 !SQ P02990
50454 ! eukaryotic and archaeal homologue of EF-Tu
105681 !SQ P35021
107617 !SQ P32324
98302 ! structural genomics
50458 ! the C-terminal domain 4 has the same fold as domain 2; it probably binds fMet-tRNAfmet
25718 ! domain 4 only
104803 !SQ O74718
104806 !SQ O74718
104809 !SQ O74718
110227 ! stand-alone protein related to this domain
109571 !SQ Q8U2D2 18-108 # ! Structural genomics target
50462 ! superfamily fold is elaborated with additional structures
105320 !SQ P20279
25719 ! CA-atoms only
50464 ! barrel, closed; n=6, S=10; greek-key
50465 ! probably related to the second domain and its superfamiy by a circular permutation
103901 !SQ P02990
50472 ! eukaryotic and archaeal homologue of EF-Tu
105682 !SQ P35021
98303 ! structural genomics
104804 !SQ O74718
104807 !SQ O74718
104810 !SQ O74718
108871 !SQ P39179 # ! Structural genomics target
92089 ! structural genomics
109468 !SQ Q9WY54
109466 !SQ Q9WY54
109460 !SQ Q9WY54
109458 !SQ Q9WY54
108838 !SQ P27248 # ! Structural genomics target
50474 ! barrel; n=6, S=10; greek-key
50475 ! related to the ferredoxin reductase-like FAD-binding domain
50479 ! elaborated with additional secondary structures; active as dimer
108732 !SQ Q8YMA7 # ! Structural genomics target
50482 ! different dimerization mode than in the PNP-oxidase like family
25757 ! structural genomics
101798 ! utilizes FAD rather than FMN
69278 ! core: barrel; n=6, S=10; greek-key; topologically similar to the FMN-binding split barrel
69280 ! duplication: consists of two similar barrel domains that differ by the first strand directions; the barrels are differently decorated by alpha+beta insertions
74966 ! similar to the N-terminal barrel of T4 gp27
101800 ! segment-swapped dimer forming two identical conjoint barrels (n=6, S=10) topologically similar to the FMN-binding split barrel
101804 ! TM0680a
92563 ! structural genomics
50485 ! barrel, open; n*=6, S*=10; greek-key
25765 ! CASP3
50493 ! barrel, closed; n=6, S=8; greek-key ! duplication: consists of two domains of the same fold
50509 ! Streptogrisin B 
50510 ! probable glutamic acid-specific protease
25828 ! CASP2
101809 ! glutamic acid-specific protease
109229 !SQ P04188 69-284
84517 ! catalytic domain only
105857 !SQ P31137 
105864 !SQ P31137 
108515 !SQ P31137 
93405 ! complexed with serpin
25953 ! complexed with serpin
108288 !SQ P00760
108291 !SQ P00760
105117 !SQ P00760
108294 !SQ P00760
108289 !SQ P00760
108295 !SQ P00760
108290 !SQ P00760
108299 !SQ P00760
108297 !SQ P00760
104043 !SQ P00760
108298 !SQ P00760
108296 !SQ P00760
108287 !SQ P00760
108286 !SQ P00760
108292 !SQ P00760
108293 !SQ P00760
103810 !SQ P00761
103812 !SQ P00761
107845 ! complexed with an auto catalyticaly produced native peptide from trypsin, chain P (SQ P00761 177-185) !SQ P00761
25999 ! Michaelis serpin-trypsin complex
68355 ! Michaelis serpin-trypsin complex
26052 ! delta-chymotrypsin
104044 !SQ P00766
26058 ! chymotrypsinogen C
26067 ! chymotrypsinogen A
84386 ! chymotrypsin B
26135 ! prethrombin 2
79111 ! anticoagulant slow form
26175 ! CA-atoms only
77137 ! complex with a heparin cofactor II mutant
105709 !SQ P00734 355-621
107197 !SQ P00734 328-620 !SQ P00734 328-620
103889 !SQ P00734
106737 !SQ P00734
105951 !SQ P00734
105553 !SQ P00734 333-622
105499 !SQ P00734 333-622
105407 !SQ P00734 333-622
105534 !SQ P00734 333-622
26204 ! chain K is pretrombin-2
106733 !SQ P00734 333-622
105525 !SQ P00734 333-622
26212 ! chain K is pretrombin-2
106730 !SQ P00734 333-622
74973 ! fibrinolytic enzyme component A
50544 ! multifunctional protein (synonym: CAP37, azurocidin)
50546 ! ring-like tetramer with active sites facing a central pore
103880 !SQ P08709 213-446
103841 !SQ P08709 213-466
85893 ! proenzyme
70611 ! proenzyme
50559 ! two pairs of homologous but non-identical chains
26325 ! proenzyme
104019 !SQ Q9I8X1
104020 !SQ Q9I8X1
50578 ! Xa: residues 16-121; trypsin: residues 122-246
103879 !SQ P00749 179-424 # chain B coverage; only a small part of chain A (156-178) is ordered
103877 !SQ P00749 179-424 # chain B coverage; only a small part of chain A (156-178) is ordered
103878 !SQ P00749 179-424 # chain B coverage; only a small part of chain A (156-178) is ordered
108628 !SQ P00749 179-425 
105418 !SQ P00749 179-425 
108627 !SQ P00749 179-425 
77683 ! microplasminogen
77703 ! microplasminogen
79692 ! proenzyme
79693 ! proenzyme
63791 ! new serine protease
103887 !SQ P05981 163-417
103885 !SQ P05981 163-417
105564 !SQ P14210 495-722
104528 !SQ O00187 366-686
50596 ! beta sheet in the first domain is opened rather than forms a barrel
82128 ! minimal fold; contains C-terminal extension
74979 ! contains an extra alpha-helical domain
101815 ! barrel; n=6, S=8, greek-key; similar to one trypsin-like protease barrel
101818 ! part of polyprotein 1AB; binds ssRNA
50609 ! barrel; n=6, S=8, greek-key
50614 ! barrel, closed; n=6, S=8; greek-key
50616 ! 6 domains form a ring structure which contains a barrel, closed; n=24, S=24(?)
108996 !SQ P19483
109015 !SQ P19483
109005 !SQ P00829
109024 !SQ P00829
50621 ! the barrel is decorated with additional structures
104882 !SQ Q9HTQ2
108586 !SQ Q65YW7
108574 !SQ Q65YW7
108590 !SQ Q65YW7
88683 ! barrel is open with strands 4 and 5 having swapped their positions, compared to the alanine racemase barrel
107405 !SQ Q58497 # ! Structural genomics target
107337 !SQ Q58497 # ! Structural genomics target
100669 ! structural genomics 
100694 ! structural genomics 
74981 ! barrel, closed; n=6, S=8, greek-key, partial similarity to the OB-fold
74984 ! tmRNA-binding protein; SsrA-binding protein
94192 ! complexed with tRNA domain of tmRNA
50629 ! barrel, closed; n=6, S=10, complex topology
50631 ! dimer of identical mono-domain chains, each containing (6,10) barrel
105300 !SQ P03368 69-167
105445 !SQ P03367 69-167
105309 !SQ P03367 69-167
105443 !SQ P03367 69-167
105447 !SQ P03367 69-167
105313 !SQ P03368 69-167
26560 ! synthetic tethered dimer
74274 ! synthetic tethered dimer
26614 ! synthetic tethered dimer
26712 ! CA-atoms only
80713 ! folded monomer
50646 ! duplication: consists of two similar barrel domains ! N-terminal: barrel, partly opened; n*=6, S*=10
65256 ! neutron laue diffraction structure
107844 !SQ P06026 69-393
107842 !SQ P06026 69-393
107843 !SQ P06026 69-393
50654 ! synonym: saccharopepsin
109395 !SQ P17576 1-329
26840 ! zymogen; contains propeptide at the N-terminus and swaposin domain (residues 1S-104S) inserted in between residues 247 and 248
26854 ! activation intermediate 2
109173 !SQ P56817 60-447
109174 !SQ P56817 60-447
79152 ! proenzyme
110247 ! pepsin-like protein that probably lost the protease activity
106564 !SQ Q8H0K8 22-402
106568 !SQ Q8H0K8 22-402
50676 ! core: barrel, closed; n=6, S=8; topology is similar to that of the acid proteases barrel
50678 ! inserted into the catalytic domain
99240 ! isolated (cp1) domain structure
99242 ! isolated (cp1) domain structure
83813 ! preliminary structure of ligand-free enzyme; CA-atoms only
82133 ! in the prokaryotic and mitochondrial LeuRS this domain is inserted into a different sequential position
69286 ! barrel, closed; n=6, S=8; a crossover loop topology
50684 ! barrel, closed; n=6, S=10; complex topology with crossover (psi) loops
82135 ! conserved Eng V active site residues and disulfides; better structural similarity to the ADC-like superfamily
50694 ! autocatalytic enzyme
94983 ! native precursor
26902 ! mature enzyme
95018 ! unprocessed mutant
95085 ! unprocessed mutant
95373 ! unprocessed mutant
95375 ! processed mutant
95014 ! unprocessed mutant
95016 ! unprocessed mutant
95083 ! unprocessed mutant
107847 !SQ P56065
107846 !SQ P56065
50696 ! molybdopterine enzyme
26907 ! Tungsten-substituted
50707 ! dissimilatory nitrate reductase (NAP)
105589 !SQ P09152
108812 !SQ P80563
106994 !SQ P80563
108788 !SQ P80563
106970 !SQ P80563
108764 !SQ P80563
106946 !SQ P80563
50709 ! NSF-N, the N-terminal 'functional' domain of the N-ethylmaleimide sensitive fusion protein, consists of two structural domains
50712 ! VAT-N is the N-terminal 'functional' domain of the VCP-like ATPase
93801 ! complete low resolution structure
109396 !SQ Q5BL07 13-179
50714 ! barrel, closed; n=6, S=10; complex topology
63798 ! contains additional all-beta (sub)domain in the C-terminal extension
59802 ! complexed with a 5S rRNA fragment
50720 ! duplication, consists of two barrel domains with the swapping of N-terminal strands
50722 ! barrel, closed; n=6, S=10; meander; capped at both ends by alpha-helices
50728 ! barrel, partly opened; n*=6, S*=12; meander; capped by an alpha-helix
50738 ! contains Btk zinc-binding motif
104961 !SQ  Q64096 624-958 # 98% sequence identity; note that the rat sequence Q63406 region 499-833 is 100% identical to the PDB sequence
50751 ! ARF1 Guanine nucleotide exchange factor and integrin binding protein homolog
70113 ! phosphoinositol (3,4)-bisphosphate binding PH domain
107968 !SQ P31749 1-117
107969 !SQ P31749 1-117
107967 !SQ P31749 1-117
104075 !SQ P31751 1-111
108379 !SQ Q9JID9 178-299 # ! Structural genomics target
108382 !SQ Q9ERS5 1-113 # ! Structural genomics target
108386 !SQ Q8K2Z0 256-367 # ! Structural genomics target
108389 !SQ Q8K4I3 429-551 # ! Structural genomics target
103874 !SQ O75962 1231-1535
108423 !SQ Q9BZF1 149-265 # ! Structural genomics target
108424 !SQ P42331 40-144 # ! Structural genomics target
107423 !SQ Q9NZN5 766-1138
109514 !SQ Q9NZN5 766-1138
50758 ! duplication: contains two domains of this fold
26991 ! second domain complexed with a IL-4 receptor phosphopeptide
26994 ! complexed with a phosphotyrosine peptide
26993 ! complexed to a nak peptide
86168 ! complexed with apoer2 peptide
86169 ! complexed with apoer2 peptide and PI-4,5P2
93421 ! complexed with peptide and I3P
91222 ! complexed with peptide
107789 !SQ P97465 152-254
79231 ! pseudo complex: fusion protein with a WIP peptide (res. 1-25) and a linker peptide (res. 26-30)
101836 ! close structural similarity to EVH1 domain
101837 ! decapping protein involved in mRNA degradation 
59281 ! includes first long helix
105530 !SQ P26038 4-297
82142 ! complexed with the icam-2 cytoplasmic peptide, chain B
69294 ! the neurofibromatosis 2 tumor suppressor protein
104145 !SQ P32780 1-108
50783 ! barrel, closed; n=6, S=12; mixed beta-sheet
50784 ! dimer of non-identical beta-sheet domains
50785 ! heterodimer of two homologous chains
50788 ! core: barrel, closed; n=7, S=8; complex topology
50799 ! barrel, closed; n=7, S=10; complex topology
50801 ! this domain interrupts beta/alpha-barrel domain ! C-terminal domain is alpha/beta
101844 ! Pfam 03473
93465 ! structural genomics
92546 ! structural genomics
92554 ! structural genomics
50808 ! barrel, closed; n=7, S=10; order: 1234765; strands 1 and 5 are parallel to each other
50809 ! an HTH motif connects strands 4 and 5
66178 ! complexed with a DNA ligase IV peptide
27077 ! CASP4
89359 ! barrel, closed; n=7, S=10; complex topology
89361 ! Pfam 01521; Iron-sulfur cluster scaffold domain
105378 !SQ P36539
86296 ! structural genomics; NESG target QR6
101851 ! barrel, closed; n=7, S=10; greek-key topology; one overside connection
100938 ! barrel, closed; n=7, S=10; complex topology
100940 ! includes C-terminal alpha-helical arm and DNA encircling insertion
100943 ! includes C-terminal alpha-helical arm and DNA encircling insertion
82152 ! core: barrel, closed; n=7, S=12; meander
82155 ! duplication: tandem repeat of four FAS1 domain
81116 ! two C-terminal FAS1 domains
50813 ! barrel, closed or opened; n=8, S=12; meander
50814 ! bind hydrophobic ligands in their interior
50815 ! barrel, closed; n=8, S=12, meander
50821 ! C-termini swapping dimer
108149 !SQ P02754
27125 ! CASP4
27138 ! CASP3
89364 ! activated expression by the myc oncogene
84475 ! engineered variant diga16
84641 ! engineered variant diga16 in complex with digitoxigenin
91527 ! engineered variant flua in complex with fluorescein
84622 ! engineered variant diga16 in complex with digoxigenin
61733 ! C1 subunit
98394 ! C2 subunit
60806 ! A1 subunit
98472 ! A1 subunit
70214 ! A1/A2 dimer
101861 ! bacterial lipocalin 
104189 !SQ Q26241
104126 !SQ Q26241
106108 !SQ Q94734 22-205
106110 !SQ Q94734 22-205
106105 !SQ Q94734 22-205
106109 !SQ Q94734 22-205
106104 !SQ Q94734 22-205
106106 !SQ Q94734 22-205
106107 !SQ Q94734 22-205
106103 !SQ Q94734 22-205
107569 !SQ Q94734
50847 ! ten-stranded meander beta-sheet folded upon itself ! relates to the common fold by opening the barrel and insertion of beta-hairpin
60293 ! heart-type
105406 !SQ P02693 ! stable and compact all-beta-sheet variant
27181 ! helix-less variant
59780 ! complexed with oleic acid
107180 !SQ P15090
107178 !SQ P15090
27213 ! CASP1
108902 !SQ P29498
108903 !SQ P29498
50872 ! topology permutation: strands 2 and 3 swapped their positions in the barrel
101863 ! bacterial metal-binding, lipocalin-like protein
107429 !SQ P76344 # ! Structural genomics target
105348 !SQ P76344 # ! Structural genomics target
101866 ! bacterial proteins with a fatty acid binding protein-like fold
96741 ! structural genomics
50875 ! barrel, closed; n=8, S=10; meander
90658 ! complexed with miniprotein MP-2, chains E, F, G and H
83650 ! complexed with miniprotein MP-2, chains C and D
83648 ! complexed with miniprotein MP-2, chains C and D
83654 ! complexed with miniprotein MP-1, chains E, F, G and H
85039 ! mutant with osteopontin hexapeptide insertion including rgd
85017 ! mutant with insertion of fibronectin hexapeptide, including rgd
27325 ! circular permuted streptavidin e51/a46
27394 ! circular permuted streptavidin e51/a46
101869 ! cysteine protease inhibitor; topology permutation: strand 3 is replaced with the N-terminal extra strand
95304 ! complexed with staphopain
50888 ! duplication: both domains have this barrel fold
101877 ! structural genomics
50890 ! barrel, closed; n=8, S=10; complex topology
78682 ! complexed with calcineurin and cyclosporin (chain D and H)
91503 ! complexed with a 30-residue peptide from U4/U6 snRNP 60kda protein, chain B
63814 ! the other domain is formed by TPR repeats
108452 !SQ P20752
108471 !SQ P20752
27512 ! see also PDB entry 1CSA
110278 ! lacks the N-terminal strand of cyclophilin but the beta-barrel (7,10) remains closed; corresponds to the C-terminal part of Pfam 05913
109498 !SQ Q81HJ5
50903 ! barrel, closed; n=8, S=10; one overside connection
50904 ! duplication: N- and C-terminal halves are related by pseudo dyad
50906 ! an oncogene product involved in T-cell prolymphocytic leukemia
50908 ! involved in T cell malignancies
63816 ! barrel, closed; n=8, S=10; mixed sheet; two overside connections
106291 !SQ Q9S446 61-206
106285 !SQ Q9S446 61-206
106282 !SQ Q9S446 61-206
105130 !SQ Q81L49
50910 ! barrel, partly open; n*=8, S*=10; one psi loop
70300 ! repeat 11, IGF-II binding domain
59305 ! repeat 11, IGF-II binding domain
76278 ! repeat 11, IGF-II binding domain
70301 ! repeat 11, IGF-II binding domain
104495 !SQ P08169 49-476
106132 !SQ P08169 49-476
106123 !SQ P08169 49-476
50915 ! dimer of two non-identical subunits; forms two similar barrels, n=8, S=10 each, that are fused together with the formation of third barrel, n=6, S=8
50922 ! consists of four 4-stranded beta-sheet motifs; meander
50925 ! duplication: consists of two domains of this fold
27529 ! C-terminal domain
50933 ! consists of five 4-stranded beta-sheet motifs; meander
101884 ! Glycosyl hydrolase family 32
108649 !SQ Q9X0V2 # ! Structural genomics target
101887 ! distorted propeller with an alpha helix inserted between the second and third blades
101888 ! Pfam 06079
50938 ! consists of six 4-stranded beta-sheet motifs; meander
50948 ! contains incomplete beta-barrel subdomain inserted in the second blade
50950 ! contains 2 additional domains of ConA-like fold
109040 !SQ P37060
109037 !SQ P37060
105151 !SQ Q26966
105147 !SQ Q26966
105149 !SQ Q26966
104167 !SQ Q7SIG4
100240 ! direct evolution; rabit-human sequence hybrid
69304 ! possibly related to the second domain of tricorn protease (a distorted 7-bladed beta-propeller)
101899 ! Pfam 01436
101904 ! beta-pinwheel, a variant of beta-propeller fold; unlike an canonical beta-propeller, strands 1 and 4 of each four-strand repeat unit are in one blade whereas strands 2 and 3 are in the next blade 
50964 ! consists of seven 4-stranded beta-sheet motifs; meander
50967 ! N-terminal domain is a jelly-roll sandwich ! C-terminal domain is Immunoglobulin-like
106294 !SQ Q01745 42-680
69308 ! sequence identical to that of <i>Dactylium dendroides</i>
82166 ! more regular propeller with clear sequence repeats
69309 ! less regular propeller with imperfect sequence repeats; quinone cofactor is a tryptophan derivative in another subunit
50970 ! less regular propeller without notable sequence repeats; quinone cofactor is a tryptophan derivative in another subunit
50978 ! also contains 8-bladed propellers
82169 ! 8-bladed beta-propeller without perfect 8-fold symmetry
89378 ! 14 repeats are arranged into two seven-bladed beta-propeller domains swapped with the N-terminal strands
105889 !SQ Q02793
110289 ! possibly related to the WD-repeat family; both sequence similarity between the blades and the WD40 repeat signature are very weak
107667 !SQ P26449
50985 ! two families are clearly related but differ by the number of strands per blade
61571 ! complexed to Ran
69315 ! lacks the outer strands
99917 ! complexed with peptide tlpwdlwtt from amphiphysin
27667 ! complex with clathrin-box peptide of B-adaptin 3
27669 ! complex with clathrin-box peptide of B-adaptin 3
108947 !SQ P23687
108945 !SQ P23687
69322 ! distorted 7-bladed beta-propeller fold; possibly related to the N-terminal domain of tricorn protease (a 6-bladed beta-propeller)
97503 ! structural genomics
101912 ! irregular 7-bladed beta-propeller with a large insertion in the fifth blade
101913 ! Pfam 01403
105565 !SQ P08581 40-564
104533 !SQ O08665 26-520
110296 ! duplication: # two beta-propeller domains are swapped with the N-terminal strands; similar domain arrangment to the Actin interacting protein 1 (scop_pr 89378) 
110297 ! contains at least 9 BNR/Asp-box repeats (Pfam 02012) usually associated with the 6-bladed propeller Neuraminidases (scop_sf 50939)
105921 !SQ Q8J0D2
50997 ! consists of eight 4-stranded beta-sheet motifs; meander ! also found in some members of the WD40-repeat superfamily
69326 ! fused with the C-terminal cytochrome c domain
51006 ! the N-terminal domain is cytochrome c-like
51007 ! formerly <i>Thiosphaera pantotropha</i>
107071 !SQ P27487
104876 !SQ P27487
107112 !SQ P27487
90783 !SQ P27487 
107735 !SQ P27487
109049 !SQ P27487
51010 ! folded sheet; greek-key
51011 ! this domain is C-terminal to the catalytic beta/alpha barrel domain
51012 ! this domain follows the catalytic beta/alpha barrel domain
107759 !SQ P00691
51018 ! contains two more all-beta domains in C-terminal region, Immunoglobulin-like and trasthyretin-like
108319 !SQ P05618
108335 !SQ P05618
108311 !SQ P05618
108327 !SQ P05618
107629 !SQ 04746
107624 !SQ 04746
107632 !SQ 04746
82175 ! homologous to Maltogenic amylase
101917 ! protein shares similar domain organization with maltogenic amylases but differs in the spatial arrangement of its domains
51038 ! single beta-sheet; probable result of a decay of the common-fold
51040 ! single beta-sheet; probable result of a decay of the common-fold
75021 ! alpha-N-acetylgalactosaminidase
89387 ! alpha-galactosidase
101919 ! alpha-galactosidase A
110300 ! Alpha-galactosidase agl1
106162 !SQ Q92456
82181 ! the catalytic domain of this protein is similar to that of the bacterial beta-amylase
101920 ! single beta-sheet; probable result of a decay of the common-fold
89388 ! interrupted by the catalytic domain; the C-terminal core is similar to the alpha-amylase domain
89389 ! glycosyl hydrolase family 30; the N-terminal extension wraps around the C-terminal core 
101924 ! glycosyl hydrolase family 51 
101926 ! glycosyl hydrolase family 39
101928 !  glycosyl hydrolase family 29; beta-sheet forms a closed beta-barrel (n=8, S=10)
101930 ! TM0306
51044 ! core: 3-stranded meander beta-sheet
61967 ! complexed with human tau phosphothreonine peptide, chain A
61966 ! complexed with cdc25 phosphothreonine peptide, chain A
61785 ! complexed to renac bp2 peptide
66888 ! in complex with gtppppytvg peptide
68358 ! complexed to acetyl-plppy
68357 ! complexed to n-(n-octyl)-gpppy-nh2
68206 ! in complex with gtppppytvg peptide
82183 ! duplication: contains two WW domains connected by a helical linker
110301 ! duplication: contains two WW domains connected by a helical linker
107078 !SQ Q9Y0H4 474-554
51063 ! small mixed beta-sheet, 4 "generalized" strands
110303 ! coiled antiparallel beta-sheet of 5 strands, order 51324; complex topology, crossing loops
105986 !SQ P59595 45-181
63839 ! twisted meander beta-sheet of 6 strands
101935 ! core: twisted 7-stranded beta-sheet (half-barrel) of complex topology
101940 ! core: twisted 7-stranded beta-sheet (half-barrel)
101942 ! transcription factor domain; Pfam 02365, NAM
51068 ! single sheet; 10 strands
27954 ! S-glutathiolated
62889 ! extracellular domain
62887 ! extracellular domain
97534 ! extracellular domain
97532 ! extracellular domain
89391 ! 11 stranded sheet partly folded in a corner-like structure filled with a few short helices
51080 ! single sheet; 16 strands; meander
51086 ! single sheet formed by beta-hairpin repeats; exposed on both sides in the middle
51087 ! 21 stranded sheet partly folded upon itself at the ends
94112 ! C-terminal, "globular" region only (of 12 strands)
82185 ! 11+ stranded sheet partly folded upon itself at the C-end
80121 ! truncated from N-terminus
81251 ! truncated from N-terminus
80123 ! truncated from N-terminus
79483 ! truncated from N-terminus
51091 ! consists of 3 4-stranded sheets; strands are parallel to the 3-fold axis ! duplication: has internal pseudo threefold symmetry
107177 !SQ Q38723 64-217 95% sequence identity
107188 !SQ Q38723 64-217 95% sequence identity
108486 !SQ Q7M1T4
108488 !SQ Q7M1T4
51109 ! consists of 3 4-stranded sheets; strands are perpendicular to the 3-fold axis ! duplication: consists of two domains of this fold
51117 ! duplication: consists of two beta-prism II domains
28011 ! low resolution structure
51125 ! superhelix turns are made of parallel beta-strands and (short) turns
51120 ! superhelix turns are made of two short strands each
51121 ! duplication: halfturs of beta-helix are sequence and structural repeats; binds calcium ions between the turns
51122 ! The catalytic N-terminal domain belong to the "zincin" superfamily
51123 ! alkaline protease
51124 ! serralysin
82189 ! protease C
82190 ! psychrophilic alkaline protease
51126 ! superhelix turns are made of 3 strands each
28021 ! CA-atoms only
51132 ! Low-molecular weight high-alkaline enzyme
28025 ! CASP2
28030 ! CASP3
51146 ! synonym: Flavobacterium heparinum
103934 !SQ Q46079 27-506
101952 ! type L pectate lyase, pel9a
28036 ! CASP4
51156 ! superhelix turns are made of two short strands each
63848 ! superhelix turns are made of three short strands each
69338 ! Central domain (residues 423-780) may be a rudiment form of the FMN domain
69340 ! superhelix turns are made of two strands each
101960 ! superhelix turns are made of two very long strands each
100641 ! structural genomics
51160 ! superhelix turns are made of parallel beta-strands and (short) turns
51161 ! superhelical turns are made of three short strands; duplication: the sequence hexapeptide repeats correspond to individual strands
51165 ! contains extra N-terminal 3-helical domain
69344 ! streptogramin A acetyltransferase 
28063 ! truncated form after R331
28065 ! truncated form after R331
51174 ! archaeal hexapeptide repeat proteins
105994 !SQ P43886 1-241 # N-terminal all-alpha subdomain (1-137; Pfam 06426)
105992 !SQ P43886 1-241 # N-terminal all-alpha subdomain (1-137; Pfam 06426)
105363 !SQ P43886 1-240 # ! Structural genomics target
105997 !SQ P43886 1-241 # N-terminal all-alpha subdomain (1-137; Pfam 06426)
106347 !SQ P05796
51177 ! superhelical turns are made of three short strands
51179 ! there are different numbers of superhelical turns (and sequence repeats) in different isoforms
73411 ! isoform 337
78774 ! isoform 501
101967 ! superhelical turns are made of two short strands
51181 ! one turn of helix is made by two pairs of antiparallel strands linked with short turns ! has appearance of a sandwich of distinct architecture and jelly-roll topology
51184 ! synonym: dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase
103941 !SQ O52806
89404 ! Type II phosphoglucose isomerase
92519 ! structural genomics
84624 ! structural genomics
86623 ! structural genomics
100797 ! structural genomics
63853 ! Metal (manganese)-binding protein with oxalate oxidase and superoxide dismutase activities; homohexamer
51188 ! duplication: consists of two germin-like domains spatially arranged as subunits in the RmlC dimer; trimer is similar to the germin hexamer
28089 ! CA-atoms only
107877 !SQ P25974
107883 !SQ Q7XXT2 204-621
75033 ! duplication: consists of two germin-like metal-ion binding domains
101979 ! Pfam 05899; formerly pfam06038  ! duplication: consists of two germin-like domains
97288 ! structural genomics 
98963 ! structural genomics; NESG target PAR14
105452 !SQ Q82ZQ3 # ! Structural genomics target
105497 !SQ Q9RV77 # ! Structural genomics target
101984 ! Share a common two-domain fold with the 7S protein; there is a metal-binding site in the N-terminal domain similar to the metal-binding site of germin
101985 ! Bcl-3 and nuclear factor I-interacting protein
75035 ! Share a common two-domain fold with the 7S protein; there is a metal-binding site in the N-terminal domain similar to the metal-binding site of germin
51191 ! Share a common two-domain fold with the 7S protein; there is a metal-binding site in the N-terminal domain similar to the metal-binding site of germin
51193 ! contains insert all-alpha subdomain; residues 152-266
51194 ! Share a common two-domain fold with the 7S protein; there is a metal-binding site in the C-terminal domain similar to the metal-binding site of germin
78606 ! NMR-derived model
110318 ! duplication: consists of two germin-like domains
109521 !SQ Q46938 1-266
51197 ! Iron and ketoglutarate-dependent enzymes; elaborated version of this common fold
51198 ! common fold is rather distorted
28117 ! Ip1 - Fe complex
108183 !SQ P05326
28119 ! monocyclic sulfoxide - Fe complex
63856 ! unknown function
84190 ! structural genomics
59279 ! iron form
59277 ! apo form
76572 ! complex with HIF-1 alpha fragment peptide
76574 ! complex with HIF-1 alpha fragment peptide
76576 ! complex with HIF-1 alpha fragment peptide
51207 ! heme-binding domain
51210 ! Pfam 00027
92506 ! structural genomics ! DNA-binding domain (res. 130-213) is disordered in this structure 
51213 ! duplication: consists of two similar domains
104978 !SQ P00514 109-376
82197 ! duplication: two homologous domains of this fold are separated in the sequence by a DEP domain
101993 ! potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel
51217 ! contains an alpha-hairpin in the C-terminal extension
81653 ! a distorted variant of double-helix
106473 !SQ P04191
108580 !SQ P04191
106477 !SQ P04191
75858 ! Structure in the absence of calcium ions
75892 ! Structure in the e2 state
51219 ! shorter variant of double-helix; assembles in large ring-like structures containing from 9 to 11 domains
51220 ! oligomeric ring consists of 11 single-domain subunits 
101995 ! duplication: there are three structural repeats per subunit; nine domains per ring-like trimer
94673 ! structural genomics; NESG target DR2 
69348 ! (homo)trimer; each chain donates 3 beta-strands per turn of the helix
88691 ! includes the N-terminal cap (sub)domain
51224 ! trimer formed by the interlocking beta-hairpin repeat units
108253 !SQ P10104 
108259 !SQ P10104 
101998 ! trimer; contains two different beta-prism-like domains connected by an linker subdomain of less regular structure
69359 ! Trp-rich beta-hairpin repeat units form helical structures of 3 units per turn
51229 ! sandwich of half-barrel shaped beta-sheets
51230 ! 7 to 8 strands in 2 beta-sheets
51238 ! component of the pyruvate dehydrogenase complex
51247 ! probable rudiment form of the biotinyl-carrier domain
51248 ! subunit of acetyl-CoA and pyruvate carboxylases 
108701 !SQ Q9X0X7 # ! Structural genomics target
51261 ! half-barrel sheet of 8 strands sandwiched with two 3-stranded sheets
51266 ! synonym: enzyme IIa-glc
102006 ! Peptidase family M23; contains extra N-terminal, non-conserved beta-sheet subdomain
110324 ! rudiment single hybrid fold with a permuted topology
110325 ! Pfam 01016; different 
108431 !SQ P84123 # ! Structural genomics target
51268 ! double-stranded ribbon sharply bent in two places; the ribbon ends form incomplete barrel; jelly-roll
51269 ! duplication: consists of two structural repeats related by pseudo dyad
51273 ! duplication: intramolecular dimer
28311 ! N-Terminal domain with a linker portion
28316 ! N-Terminal domain with a linker portion
108830 !SQ P39625 # ! Structural genomics target
82199 ! duplication: the core is composed of two structural repeats similar to (circularly permuted) repeats of AFPIII ! also contains a substrate-binding alpha+beta subdomain inserted in the core
82200 ! contains metal-binding preSET and postSET domains
94599 ! complexed with histone H3 peptide
82203 ! ortholog of Dim-5
82207 ! consists of SET domain only; dimeric
106764 !SQ P03712
28328 ! CASP1
69367 ! fused with gamma subunit
106351 !SQ Q03555 350-768 # structure on the N-terminal domain (1-201) is also known (1ihc; scop_sp 64101)
51283 ! forms tight trimer through an additional beta-sheet in each subunit ! subunit beta-sheets are orthogonally packed around the three-fold axis
105454 !SQ P06968
105021 !SQ P06968
105020 !SQ P06968
106117 !SQ P06968
79404 ! structural genomics ! CASP5
89425 ! elaborated fold with additional structures
89426 ! synonym: Methanocaldococcus jannaschii
51289 ! similar to dUTPase in fold and trimeric assembly
82214 ! multisheet protein with a mixture of beta-sandwich and beta-prism features
82217 ! pore-targeting domain
89427 ! multisheet protein containing partial beta-propeller and beta-sandwich regions
89430 ! synonym: receptor-binding protein p2
89432 ! multisheet protein with a mixture of beta-sandwich and beta-barrel features
51293 ! complex fold made of five beta-hairpin units and a b-ribbon arc
51294 ! duplication: contains two intertwined structural repeats
51299 ! also contains a homing endonuclease and DNA-binding domains
76262 ! domain I only
77178 ! contains the N and C extein propeptides
28377 ! miniprecursor; a few extra residues are added at the N-terminus
107949 !SQ P17255 284-737 ! complexed with the ligated extein segment (SQ P17255 281-283,738-741), chains C and D
51303 ! miniintein lacking the homing endonuclease domain
102011 ! miniintein lacking the homing endonuclease domain
51305 ! complex fold made of several coiled beta-sheets; contains an SH3-like barrel
51308 ! self-processed fragment of UmuD SOS response protein
51312 ! contains additional all-beta subdomain inserted in the superfamily fold
68702 ! apo-enzyme
106623 !SQ P00803 81-324
69368 ! complex fold made of several coiled beta-sheets
69370 ! Pfam 03515
51315 ! complex fold made of several coiled beta-sheets
51316 ! duplication: tandem repeat of two similar structural motifs
51317 ! contains zinc-binding site
63873 ! contains an insertion of alpha helical hairpin; lacks zinc-binding site
107424 !SQ P84152 # ! Structural genomics target
51321 ! complex fold
51322 ! duplication: tandem repeat of two homologous motifs made three stranded beta-sheet and beta-hairpins
28395 ! swapped dimer
74152 ! swapped dimer
73576 ! swapped dimer
78650 ! swapped dimer, complexed to a synthetic hexamannoside
78652 ! swapped dimer, complexed to oligomannose-9 (man-9)
71528 ! swapped dimer
73580 ! swapped dimer
28396 ! CASP3
79717 ! circular-permuted variant
82219 ! complex fold; consists of two intertwined subdomains
82222 ! a penicillin-binding protein with carboxypeptidase activity
63876 ! complex fold
63877 ! duplication: contains two similar sub domains connected by a structured linker
51326 ! complex fold made of bifurcated and partly folded beta-sheet
51331 ! complex fold made of bifurcated and coiled beta-sheets
107334 !SQ Q80B71 1-193 # includes the N-terminal alpha-helical region (1-90), binding the E1 helicase domain
28405 ! contains additional N-terminal (sub)domain; alpha-hairpin
97157 ! contains additional N-terminal (sub)domain; alpha-hairpin
97152 ! contains additional N-terminal (sub)domain; alpha-hairpin
63881 ! complex fold made of bifurcated and coiled b-sheets
106352 !SQ Q03555 350-768 # structure on the N-terminal domain (1-201) is also known (1ihc; scop_sp 64101)
51337 ! pseudobarrel; mixed sheet of 7 strand folded upon itself and "buckled" by two beta-turns
51338 ! this domain is interrupted by the catalytic beta/alpha barrel domain
28412 ! CASP1
90955 ! structural genomics; NYSGR target T-45
87696 ! structural genomics
77089 ! structural genomics
104201 !SQ P39377
104209 !SQ P39377
104205 !SQ P39377
82229 ! TM0814
80760 ! structural genomics ! CASP5
51343 ! pseudobarrel: sandwich of two sheets packed at a positive interstrand angle and interconnected with many short turns
51346 ! delta subunit in mitochondria
60757 ! the rest of subunit structure is disordered
81625 ! pseudobarrel; capped on both ends by alpha-helices
96893 ! bound to 5,6-Dihydrouracil (DhU) containing DNA
75912 ! covalent-DNA intermediate
75909 ! bound to abasic-site containing DNA
75921 ! DNA estranged guanine mismatch recognition complex
75918 ! DNA estranged thymine mismatch recognition complex
96890 ! bound to 8-Oxoguanine (OxoG) containing DNA
75915 ! DNA end-product structure
75876 ! covalently trapped with DNA
106788 !SQ P42371
104165 !SQ P42371
104162 !SQ P42371
104191 !SQ P42371
104519 !SQ P50465
104522 !SQ P50465
104516 !SQ P50465
106773 !SQ Q96FI4 1-333
89441 ! pseudobarrel; capped at one end by an alpha-helix
85787 ! structural genomics
89446 ! pseudobarrel; capped on both ends by alpha-helices
89447 ! members of this superfamily are known or predicted to have DNA-binding function
89448 ! forms intertwined homodimer
85144 ! complex with camelid antibody VHh
88401 ! complex with MazF poison protein
54743 ! dimeric fold similar to MazE; the DNA-binding site is similar to the conserved surface site of MraZ  
38765 ! obsolete incorrect structure; superseded by 1Z0R; see also 1YFB and 1YSF
102020 ! duplication: contains two interlocking repeats of similar sequence arranged as subunits in the MazE homodimer  
91515 ! structural genomics
91525 ! structural genomics
91523 ! structural genomics
88696 ! pseudobarrel; mixed folded sheet of 5 strands; order 13452; strand 1 and 3 are parallel to each other
88698 ! RNA-binding domain
88701 ! the last of the 3 additional C-terminal domains to the TGT-like domain
102025 ! this protein is related to the C-terminal part (domains C2 and C3) of Archaeosine tRNA-guanine transglycosylase
96042 ! structural genomics
106495 !SQ Q9Y221 # RL 1Q7H|Q9HIB8 (B-E); 1J2B|O58843 (361-582)
63801 ! contains extra structures; some similarity to the PK beta-barrel domain
100716 ! structural genomics
86393 ! structural genomics
100686 ! structural genomics; domains of B and D chains are partly disordered 
110339 ! DUF984: Pfam 06171
106542 !SQ Q82ZD1 # ! Structural genomics target
102030 ! pseudobarrel; some similarity to OB-fold
63886 ! non-globular proline-rich hairpin
51350 ! contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 ! the first seven superfamilies have similar phosphate-binding sites
106061 !SQ P00940
106066 !SQ P00940
105879 !SQ P00940
106074 !SQ P00940
105980 !SQ P00940
106021 !SQ P00940
105887 !SQ P00940
105985 !SQ P00940
28488 ! modified substrate binding site
28479 ! monomeric mutant structure
28481 ! different dimerisation mode mutant
106032 !SQ P52270
28500 ! structure in hexane
80007 ! ultra-high resolution structure
109034 !SQ Q8NKN9
51367 ! structural evidence for the gene duplication within the barrel fold
100646 ! structural genomics
107233 !SQ P74061
28541 ! complex with UMP
28549 ! complex with 6-azaUMP
28558 ! complex with 6-hydroxyuridine 5'-phosphate (BMP)
105837 !SQ P39304
105839 !SQ P39304
105835 !SQ P39304
105841 !SQ P39304
51383 ! merged in bifunctional enzyme with IPG synthase
51386 ! merged in bifunctional enzyme with PRA isomerase
71633 ! stability mutant containing an engineered disulfide bridge
75052 ! TM0140
71583 ! structural genomics
28590 ! CASP4
109602 !SQ Q8U192 ! Structural genomics target
51399 ! PyrD subunit
102040 ! At1G76680
100813 ! structural genomics
108906 !SQ P71278
108905 !SQ P71278
108907 !SQ P71278
51406 ! two other domains are alpha/beta Rossmann-like fold and beta/beta/alpha fold
51409 ! N-terminal domain homologous to cytochrome b5
106156 !SQ P00175
106154 !SQ P00175
106152 !SQ P00175
69381 ! Central domain (residues 423-780) may be a rudiment form of the FMN domain
102044 ! Dihydrouridine synthase (Dus) homologue; contains extra C-terminal alpha-helical domain
100693 ! structural genomics
102046 ! provisional classification; it is not known whether this protein binds FMN or not
100785 ! structural genomics
51412 ! The phosphate moiety of substrate binds in the 'common' phosphate-binding site
28638 ! contains two CBS domains inserted into the common fold
79028 ! there two CBS domains in the disordered region 102-221
79027 ! there two CBS domains in the disordered region 108-219
28639 ! there two CBS domains in the disordered region 102-221
88315 ! there are two CBS domains in the disordered region 100-230
91250 ! there two CBS domains in the disordered region 107-221
91251 ! there two CBS domains in the disordered region 102-221
91249 ! there two CBS domains in the disordered region 102-221
91256 ! there two CBS domains in the disordered region 102-221
84688 ! there are two CBS domains in the disordered region 101-230
84163 ! contains two CBS domains inserted into the common fold, residues 111-231
28641 ! contains two CBS domains inserted into the common fold, residues 112-231
63244 ! contains two CBS domains inserted into the common fold, residues 113-232
51419 ! circular permutation of the canonical fold: begins with an alpha helix and ends with a beta-strand
104883 !SQ Q9HTQ2
108587 !SQ Q65YW7
108575 !SQ Q65YW7
108591 !SQ Q65YW7
89457 ! most similar to eukaryotic ODC
107406 !SQ Q58497 # ! Structural genomics target
107338 !SQ Q58497 # ! Structural genomics target
51428 ! structure from BNL's human proteome project
51431 ! Common fold covers whole protein structure
28679 ! different isozyme (?)
106391 !SQ P15121
109526 !SQ P15121
109524 !SQ P15121
109525 !SQ P15121
106390 !SQ P15121
28693 ! CA-atoms only
69383 ! bile acid binding protein
102049 ! Aldo-keto reductase family 1 member c1 
96482 ! structural genomics 
102051 ! Aldo-keto reductase family 1 member c3
99806 ! apo form
102054 ! vegetative protein 147, VEG147, AKR11A
102056 ! General stress protein 69, GSP69, AKR11B
84675 ! structural genomics
104540 !SQ P80508
51446 ! members of the family may contain various insert subdomains ! in alpha-amylases and closer relatives this domain is usually followed by a common all-beta domain
63903 ! the N-terminal 300 residues are from B. amyloliquefaciens
107760 !SQ P00691
63904 ! similar to bacterial alpha-amylase; contains larger insertion domain
51452 ! contains two more all-beta domains, one is Immunoglobulin-like and the other is trasthyretin-like
108320 !SQ P05618
108336 !SQ P05618
108312 !SQ P05618
108328 !SQ P05618
51458 ! contains Ca2+-binding subdomain, residues 100-170
107630 !SQ 04746
107625 !SQ 04746
107633 !SQ 04746
51465 ! contains an additional N-terminal domain
82240 ! homologous to Maltogenic amylase
102058 ! protein shares similar domain organization with maltogenic amylases but differs in the spatial arrangement of its domains
82242 ! elaborated with several large insertions in the common fold
76843 ! insertions: res. 129-189, 285-417 and 454-562
51468 ! contains an additional N-terminal domain
102060 ! sequence and close structural relationship to amylosucrase; variations in the C-terminal domain fold
75065 ! alpha-N-acetylgalactosaminidase
89468 ! alpha-galactosidase
102062 ! alpha-galactosidase A
110349 ! Alpha-galactosidase agl1
106163 !SQ Q92456
51478 ! 4-alpha-glucanotransferase; single-domain amylase with several insertions in the common fold
51479 ! synonym: <i>Thermus thermophilus</i>
82246 ! the catalytic domain is very similar to that of the bacterial beta-amylase; but contains a typical alpha-amylase extra domain
51485 ! protein contains additional starch-binding domain
51481 ! Common fold covers whole protein structure
108303 !SQ P10538
108304 !SQ P10538
51487 ! consist of a number of sequence families
51489 ! belongs to family F
104839 !SQ P40943
104840 !SQ P40943
102063 ! intra-cellular xylanase
51490 ! belongs to family 10
100838 ! structural genomics
109159 !SQ O85465 30-329 
109158 !SQ O85465 30-329 
60165 ! complexed with cellobiose
102068 ! mannosyl-oligosaccharide glucosidase
89471 ! Myceliophthora thermophila is the anamorph name whilst Thielavia heterothallica is the teleomorph name
104380 !SQ P00722
104360 !SQ P00722
108207 !SQ P26514 43-344
108206 !SQ P26514 43-344
108208 !SQ P26514 43-344
108209 !SQ P26514 43-344
28891 ! CA-atoms only
28903 ! CASP1
76732 ! ultra high resolution structure
28907 ! X-ray determined sequence differs from that in other entries
51519 ! N-terminal domain; fused with a ricin A-like beta-trefoil domain
108401 !SQ Q7SI98 ! Artificial chimera
51520 ! synonym: beta-1,4-glycanase Cex
106732 !SQ Q00177
102071 ! Endo-beta-1,4-xylanase
89473 ! acid-beta-glucosidase; glycosyl hydrolase family 30; contains additional beta-domain similar to one found in alpha amylases
102073 ! overall domain organization is similar to the homologous glucosylceramidase
102075 ! glycosyl hydrolase family 51 
102077 ! glycosyl hydrolase family 39
102079 !  glycosyl hydrolase family 29; contains additional beta-barrel with a topological similarity to the C-terminal domain of alpha amylases
102081 ! TM0306
51524 ! Cyanogenic beta-glucosidase
108203 !SQ P49235
28945 ! Dhurrinase
108199 !SQ Q41290
108200 !SQ Q41290
28947 ! CASP1
109157 !SQ Q08638
108078 !SQ P22498
108074 !SQ P22498
108076 !SQ P22498
108070 !SQ P22498
108072 !SQ P22498
51534 ! glycosylase family 18
106731 !SQ Q8L5C6
106790 !SQ Q8L5C6
51537 ! close relation of hevamine, may bind chitin
28988 ! X-ray sequence
89480 ! secreted during involution
104041 !SQ P30922
104784 !SQ Q6TMG6
105946 !SQ Q6TMG6
106860 !SQ Q7YS85
63912 ! Glycosyl hydrolase family 25; probably have evolved from a type II chitinase ancestor ! permutation of the common fold; strand 8 is antiparallel to the rest of the barrel
63913 ! supersedes and corrects the old structure from S. erythraeus; 0LZ6
102082 ! homologue of BH2215 from the complete Bacillus halodurans genome
98846 ! structural genomics
51550 ! Glycosyl hydrolase family 20, GH20
82253 ! Glycosyl hydrolase family 67, GH67; structurally related to GH20; contains extra C-terminal alpha-helical subdomain
82254 ! inverting reaction mechanism
51554 ! interdomain linker forms an additional, N-terminal strand
69387 ! distorted barrel lacks the second strand
110354 ! corresponds to the N-terminal part of Pfam 05913
109499 !SQ Q81HJ5
51556 ! the beta-sheet barrel is similarly distorted and capped by a C-terminal helix ! has transition metal ions bound inside the barrel
51558 ! Common fold covers the whole protein structure
104644 !SQ P56658
103890 !SQ P56658
107957 !SQ P56658
109054 !SQ P56658
29034 ! CASP1
90956 ! structural genomics; NYSGR target T-45
87697 ! structural genomics
77090 ! structural genomics
104202 !SQ P39377
104210 !SQ P39377
104206 !SQ P39377
82263 ! TM0814
80761 ! structural genomics ! CASP5
82265 ! contains small a/b subdomain inserted after strand 7; unusual for the superfamily metal coordination by Cys
102087 ! identical sequence to the <i>Pseudomonas diminuta</i> PTE
75082 ! contains all-alpha subdomain inserted after the first strand
71582 ! structural genomics
51569 ! Common fold covers whole protein structure
51570 ! the catalytic lysine forms schiff-base intermediate with substrate ! possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels
104061 !SQ P00882
82270 ! TM1559
80757 ! structural genomics ! CASP5
79699 ! structural genomics; QR15 ! CASP5
88398 ! structural genomics
84046 ! structural genomics
92505 ! structural genomics
29157 ! Schiff base intermediate
108870 !SQ Q9WXS1 # ! Structural genomics target
102092 ! putative KHG/KDPG aldolase 
100666 ! structural genomics; high-resolution structure
51588 ! probably related to class I aldolases by a circular permutation
107161 !SQ Q9L7R9 # ! Structural genomics target
109155 !SQ Q97U28
109145 !SQ Q97U28
109167 !SQ Q97U28
109163 !SQ Q97U28
51591 ! metal-dependent
51594 ! hybrid of classes I and II aldolase
109082 !SQ Q59334
105138 !SQ Q9WYH8
104155 !SQ P17579
104188 !SQ P17579
104154 !SQ P17579
92535 ! structural genomics
89496 ! gene product DmpG
105964 !SQ P96420
105058 !SQ Q70AC7 3-474
105067 !SQ Q70AC7 3-474
105074 !SQ Q70AC7 3-474
105062 !SQ Q70AC7 3-474
105236 !SQ Q70AC7 3-474
107683 !SQ Q70AC7 3-474
108831 !SQ P39625 # ! Structural genomics target
51604 ! binds metal ion (magnesium or manganese) in conserved site inside barrel ! N-terminal alpha+beta domain is common to this family
51606 ! Fold of this protein slightly differs from common fold in topology
64824 ! CASP4
106799 !SQ P09104
107103 !SQ O34508
97928 ! structural genomics
105638 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
105630 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
105622 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
105614 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
104753 !SQ Q9RYA6
51623 ! this domain is interrupted by an all-beta domain ! C-terminal domain is alpha/beta
51633 ! the common fold is decorated with many additional helices
88704 ! forms a swapped dimer
51642 ! elaborated with additional subdomains
51638 ! forms a swapped dimer; contains a PK-type metal-binding site
89501 ! Intermolecular Diels-Alderase
110375 ! non-swapped trimer
105535 !SQ Q9RUZ0 4-234
89504 ! dodecameric enzyme; a C-terminal helix exchange is observed in the M. tuberculosis enzyme but not in the E. coli enzyme
92551 ! structural genomics
92559 ! structural genomics
51647 ! contains the insert of all-beta (sub)domain and the C-terminal extension of all-alpha (sub)domain
51650 ! N-terminal domain is alpha+beta
51658 ! different families share similar but non-identical metal-binding sites
51660 ! DNA repair enzyme
71118 ! Structural genomics
71119 ! Structural genomics
72096 ! Structural genomics
79495 ! atomic resolution structure
79328 ! atomic resolution structure
107467 !SQ Q82ZC9 # ! Structural genomics target
51679 ! consists of clearly related families of somewhat different folds
51680 ! typical (beta/alpha)8-barrel fold ! heterodimer of two similar chains
29547 ! heterodimer with beta chain
29553 ! heterodimer with beta chain
29548 ! heterodimer with alpha chain
29550 ! beta2 homodimer
29552 ! beta2 homodimer
29554 ! heterodimer with alpha chain
51683 ! incomplete beta/alpha barrel with mixed beta-sheet of 7 strands
92050 ! structural genomics
107366 !SQ O34974
51690 ! incomplete beta/alpha barrel with parallel beta-sheet of 7 strands
89507 ! TM1645
86626 ! structural genomics
89508 ! Pfam 03009
86555 ! structural genomics
106672 !SQ P09394 # ! Structural genomics target
51704 ! the subunits are clearly related but only one (alpha) is active
88711 ! the subunits are clearly related but only one (alpha) is active
51715 ! contains zinc-binding subdomain
105234 !SQ P28720
107421 !SQ Q81VW8
107412 !SQ Q81VW8
107419 !SQ Q81VW8
107415 !SQ Q81VW8
107417 !SQ Q81VW8
102104 ! 5-methyltetrahydrofolate homocysteine S-methyltransferase
110384 ! duplication; consists of two related domains
107591 !SQ O50008 
107581 !SQ O50008
107609 !SQ O50008
107601 !SQ O50008
51730 ! distinct cofactor-binding mode from both FMN- and NAD(P)-linked TIM-barrel oxidoreductases; families are related by a circular permutation
75100 ! contains a UAG-encoded L-pyrrolysine residue
82283 ! Pfam 02574
102108 ! 5-methyltetrahydrofolate homocysteine S-methyltransferase
107732 !SQ O06739 # ! Structural genomics target
102114 ! common Fe-S cluster and SAM binding sites are embedded into complete or incomplete beta/alpha-barrel
102115 ! regular (beta/alpha)8 barrel
102118 ! open beta/alpha barrel decorated with additional structures
110388 ! open alpha/beta-barrel with a specific second FeS cluster-binding region corresponding to Pfam 06463
107353 !SQ P69848
107351 !SQ P69848
108659 !SQ Q9X1F0 # ! Structural genomics target
107398 !SQ P67825 # ! Structural genomics target
110399 ! shares the common phosphate-binding site with other superfamilies 
107456 !SQ O31618
51734 ! core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456 ! The nucleotide-binding modes of this and the next two folds/superfamilies are similar
51736 ! N-terminal all-beta domain defines family
29680 ! steroid-active isozyme
74532 ! glutathione-dependent formaldehyde dehydrogenase
74571 ! glutathione-dependent formaldehyde dehydrogenase
29726 ! gamma-2 isozyme
79373 ! glutathione-dependent formaldehyde dehydrogenase
29728 ! beta-1 isozyme
74608 ! glutathione-dependent formaldehyde dehydrogenase
29738 ! sigma isozyme
84932 ! glutathione-dependent formaldehyde dehydrogenase
29746 ! sigma isozyme
29750 ! glutathione-dependent formaldehyde dehydrogenase
29748 ! alpha isozyme
29756 ! sigma isozyme
100793 ! structural genomics
92645 ! structural genomics
103899 !SQ P26646 # ! Structural genomics target
29781 ! CASP4
88279 ! structural genomics ! coenzyme-binding domain only; the fragment termini approximately correspond to the family domain boundaries
100795 ! structural genomics
104478 !SQ Q04894
104159 !SQ Q04894
104303 !SQ Q04894
108344 !SQ Q9EQZ5
108348 !SQ Q9EQZ5
108340 !SQ Q9EQZ5
51751 ! also known as short-chain dehydrogenases and SDR family ! parallel beta-sheet is extended by 7th strand, order 3214567; left-handed crossover connection between strands 6 and 7
69407 ! has an UDP-galactose 4-epimerase-like structure but evolved a different function
106998 !SQ O59919
102144 ! dicarbonyl/L-xylulose reductase
87197 ! structural genomics
104660 !SQ P14061
104661 !SQ P14061
104659 !SQ P14061
80458 ! structural genomics
82294 ! peroxisomal multifunctional enzyme type 2 ! segment swapping involving a C-terminal extension to the family fold
102150 ! TM1169
92502 ! structural genomics
107841 !SQ Q9BJJ9 96-424 # fragment
108302 !SQ Q9BJJ9 96-424 # fragment
63931 ! Histidine in the active site instead of the Tyr-Lys dyad
59210 ! CASP4
102153 ! haloalcohol dehalogenase: evolved a new activity; lost the NAD-binding site
105410 !SQ Q8KN66 # list: Q8GGB8 Q9RHD6 99% identity
105411 !SQ Q8KN66 # list: Q8GGB8 Q9RHD6 99% identity
108706 !SQ Q97GQ1 # ! Structural genomics target
108734 !SQ Q9WYS2 # ! Structural genomics target
105833 !SQ Q9W3H4 # cg10964-pa
109592 !SQ Q19774
51800 ! family members also share a common alpha+beta fold in C-terminal domain
105346 !SQ P06977
89526 ! formerly Alcaligenes xylosoxidans
29993 ! CASP3
105004 !SQ P19866
105010 !SQ P19866
104998 !SQ P19866
106408 !SQ P00353
106416 !SQ P00353
104045 !SQ P44801
104286 !SQ P44801
104308 !SQ P44801
104300 !SQ P44801
104505 !SQ P44801
104294 !SQ P44801
104304 !SQ P44801
107356 !SQ P31116
108882 !SQ Q9X1K8 # ! Structural genomics target
104992 !SQ P11986
107588 !SQ O28480
108684 !SQ Q18664 # ! Structural genomics target
102161 ! myo-inositol 1-phosphate synthase-related protein
100828 ! structural genomics
104441 !SQ P45568
104468 !SQ P45568
106268 !SQ P45568
106276 !SQ P45568
104456 !SQ P45568
104733 !SQ Q9X5F2
104745 !SQ Q9X5F2
107137 !SQ P75931 # ! Structural genomics target
108682 !SQ Q9X2A2 # ! Structural genomics target
109578 !SQ Q9KKQ4
51830 ! this domain interrupts the other domain which defines family
82298 ! C-terminal binding protein 1; a dehydrogenase
51839 ! has additional C-terminal domain of the ferredoxin fold
63937 ! L-alanine dehydrogenase homologue
91970 ! complexed with dIII component
95101 ! complexed with dIII component
61472 ! complexed with dIII component
75111 ! involved in siroheme synthesis
82300 ! identical sequence to that from the <i>Thermus flavus</i> enzyme
108114 !SQ P80040
108118 !SQ P80040
108102 !SQ P80040
108106 !SQ P80040
108110 !SQ P80040
103990 !SQ O08349
103988 !SQ O08349
89531 ! TM1834
100833 ! structural genomics
107741 !SQ P54716
105314 !SQ P84135
107990 !SQ Q9X108
51868 ! the beta-sheet is extended to 8 strands, order 32145678; strands 7 & 8 are antiparallel to the rest ! C-terminal domains also show some similarity
51869 ! contains additional subdomain at the N-terminus, partly ordered
90832 ! structural genomics
69421 ! lacks all but the first helix of the C-terminal all-alpha domain
109256 !SQ P28793
109280 !SQ P28793
109268 !SQ P28793
51883 ! extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotineamide-binding site
51894 ! the two-domain organization is similar to that of aminoacid dehydrogenases, but both domains are truncated
100728 ! structural genomics
80683 ! structural genomics
86001 ! structural genomics
89540 ! MJ1084
86272 ! structural genomics
69413 ! other domains of this protein are distinct from those usually associated with the family domain
51898 ! includes C-terminal additional subdomains
108730 !SQ Q9WZ12 # ! Structural genomics target
75122 ! includes extra C-terminal alpha+beta subdomain, residues 261-336
102175 ! forms swapped dimer with C-terminal helices
102176 ! CASP5
109565 !SQ Q9X2V5
87049 ! alpha-chain only
89542 ! putative CoA-binding protein
83712 ! structural genomics; native protein
83713 ! structural genomics; cell-free system protein
110436 ! contains additional alpha+beta dimerisation subdomain mostly formed by the N-terminal meander beta-sheet
108835 !SQ O28608 # ! Structural genomics target
104018 !SQ O28608 # Rossmann-fold core (101-292) begins with an N-terminal helix and ends with a beta-strand  
51904 ! core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
51907 ! N-terminal domain is beta/alpha barrel and the middle domain is alpha/beta Rossmann-fold
51913 ! C-terminal domain is alpha+beta is common for the family
79671 ! atomic resolution structure
51922 ! structurally very similar to PHBH, but contains additional C-terminal domain of the thioredoxin-like fold
106777 !SQ Q90W54 21-504
106775 !SQ Q90W54 21-504
106779 !SQ Q90W54 21-504
51931 ! Similar to FAD-linked reductases in both domains but does not bind FAD
51932 ! the inhibition function is probably associated with an insert subdomain, residues 120-220
107916 !SQ P39958 5-446
108596 !SQ P37727
108619 !SQ P37727
51940 ! contains additional N-terminal multiheme domain
51943 ! duplication: both domains have similar folds and functions ! most members of the family contain common C-terminal alpha+beta domain
51950 ! lacks the "interface" C-terminal alpha+beta domain
30544 ! complexed with thioredoxin
59870 ! Catalytic core component only
51966 ! has a smaller C-terminal alpha+beta domain instead the "interface" domain
109172 !SQ Q5YS95 # 55% sequence identity; Nocardia farcinica TaxID:37329
51970 ! 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; Rossmann-like
51971 ! this superfamily shares the common nucleotide-binding site with and provides a link between the Rossmann-fold NAD(P)-binding and FAD/NAD(P)-binding domains
51979 ! This family is probably related to the FAD-linked reductases and shares with them the C-terminal domain fold
69427 ! domain structure is similar to that of D-aminoacid oxidase
51983 ! 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; incomplete Rossmann-like fold; binds UDP group
82316 ! TM0231
77094 ! structural genomics ! CASP5
51988 ! variant of beta/alpha barrel; parallel beta-sheet barrel, closed, n=7, S=8; strand order 1234567; some members may have fewer strands
30665 ! CA-atoms only
89551 ! putative phosphoesterase domain; contains trinuclear metal-binding site; some similarity to the metallohydrolases of TIM-barrel fold
84847 ! structural genomics
104101 !SQ P75914 # ! Structural genomics target
84848 ! structural genomics
108402 !SQ O59543 # PH1877
88713 ! in the different families beta-barrels are similarly distorted but may vary in the number of strands
89554 ! family 57 glycoside hydrolase; overall domain organization is similar to that of the alpha-mannosidase family
88714 ! family 38 glycoside hydrolase; overall domain organization is similar to that of the 4-alpha-glucanotransferase family
89557 ! the single-chain precursor is processed into 5 peptides; heavily glycosylated
99330 ! structural genomics
89559 ! variant of beta/alpha barrel; parallel beta-sheet barrel, closed, n=6, S=8; strand order 123456
86396 ! structural genomics; target SR127
51997 ! contains: barrel, closed; n=10, S=10; accommodates a hairpin loop inside the barrel
51998 ! duplication: the N- and C-terminal halves have similar topologies
51999 ! Pfam 02901; except the C-terminal ~100 residues covered by Pfam 01228
104866 !SQ Q8GEZ8
104868 !SQ Q8GEZ8
104854 !SQ Q8GEZ8
104132 !SQ Q08698
104130 !SQ Q08698
104128 !SQ Q08698
104134 !SQ Q08698
52008 ! 3 layers: b/b/a; the central sheet is parallel, and the other one is antiparallel; there are some variations in topology ! this domain is thought to be mobile in most multi-domain proteins known to contain it
52009 ! contains barrel, closed, n=7, S=10
52014 ! contains 4-helical insert domain, residues 22-144
89562 ! structural similarity and possible distant homology to the phosphohistidine domain of pyruvate phosphate dikinase
89563 ! aka MenG-like; characterized as regulator of RNase E activity A (RraA) that globally modulates RNA abundance in E. coli
89564 ! RraA homologue; (mis)annotated as a probable MenG-like demethylmenaquinone methyltransferase
86384 ! structural genomics
102194 ! RraA homologue
100731 ! structural genomics
102196 ! as (mis)annotated in the PDB entry; RraA homologue
102198 ! contains mixed beta-sheet barrel, closed n=7, S=10
102199 ! Pfam 04199; COG1878: predicted metal-dependent hydrolase
102200 ! not in the sequence database yet; closest homologue is TTE1006 from Thermoanaerobacter tengcongensis
102201 ! conflict: annotated in PDB as from Escherichia coli
52016 ! contains mixed beta-sheet barrel, closed n=7, S=10
52017 ! permutation of the domain order
52018 ! other three domains have alpha/beta folds
106331 !SQ P00907
30771 ! separately expressed fragment
30780 ! separately expressed fragment
109328 !SQ P61491
109380 !SQ P61491
30818 ! apical domain only
30821 ! apical domain only
30824 ! apical domain only
70276 ! apical domain only
70284 ! apical domain only
52037 ! 2 layers, a/b; parallel beta-sheet of 3 strands, order 123
52043 ! contains irregular N-terminal extension to the common fold
105344 !SQ P12736
63417 ! core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1234; structural similarity of the MurF and HprK extends beyond the core.
63418 ! binds UDP group
75138 ! probable phosphatase
52046 ! 2 curved layers, a/b; parallel beta-sheet; order 1234...N; there are sequence similarities between different superfamilies
52047 ! regular structure consisting of similar repeats
52049 ! duplication: consists of 16 repeats
82322 ! duplication: consists of 5 repeats
88073 ! structural genomics
52053 ! GTPase-activating protein for SpI1, ortologue of Ran ! duplication: consists of 11 repeats
52058 ! less regular structure consisting of variable repeats
52059 ! capped at the N-end with a truncated EF-hand subdomain
30869 ! chain A contains disordered non-canonical RBD domain in the N-terminal part
52068 ! duplication: consists of 5-6 partly irregular repeats
52073 ! L1 and L2 domains
74526 ! L1 and L2 domains
91377 ! complexed with TGF-alpha
86034 ! complexed with EGF
76850 ! L1 and L2 domains; complexed with EGF
52075 ! (beta-beta-alpha)n superhelix
84903 ! relaxation-based refined structure
52079 ! core: three turns of irregular (beta-beta-alpha)n superhelix
105331 !SQ P12737
105334 !SQ P12733
52086 ! core: 4 turns of a (beta-alpha)n superhelix
52088 ! Pfam 00650
102205 ! Sec14-like protein 2; contains extra C-terminal beta-sandwich domain 
104016 !SQ O76054
60627 ! phosphorylated form
60629 ! unphosphorylated form
60630 ! unphosphorylated form
106909 !SQ O32726 # 90% sequence identity
107002 !SQ O32726 # 90% sequence identity
106919 !SQ O32726 # 90% sequence identity
107009 !SQ O32726 # 90% sequence identity
108494 !SQ Q9X1F5 # TM1442
52095 ! core: 4 turns of (beta-beta-alpha)n superhelix
52100 ! includes N-terminal all-alpha subdomain
69438 ! very similar to the tail-specific protease domain; lacks the PDZ insertion domain and hydrolytic activity
69440 ! an RNA-binding homologue of enoyl-CoA hydratase
106175 !SQ Q93TU6
109257 !SQ P28793
109281 !SQ P28793
109269 !SQ P28793
89572 ! the active site is formed by two different homologous subunits or domains of this fold
89573 ! duplication: consists of two similar structural domains forming a functional domain of a larger multifunctional enzyme
109139 !SQ Q00955 1482-2196
52112 ! 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 2134
63956 ! duplication: tandem repeat of BRCT domain
104021 !SQ P38398 1755-1863 ! C-terminal domain only
91053 ! structural genomics; NESG target WR64TT; BRCT domain only
52120 ! 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 2134
52124 ! beta-subunit of the lumazine synthase/riboflavin synthase complex; 60 subunits form an icosahedral shell
52140 ! 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 2134
31021 ! CASP3
79574 ! DNA product complex
79575 ! DNA pseudo substrate complex
89578 ! gene TM0511
100845 ! structural genomics
102214 ! 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 2134
102219 ! 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 2134
52155 ! 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 2134
53222 ! core: 3 layers: a/b/a; parallel beta-sheet of 4 strands; 2134
53224 ! dimerisation domain; contains additional structures including two extra N-terminal strands in the beta-sheet
53236 ! the two-domain organization is similar to that of aminoacid dehydrogenases, but both domains are truncated
100729 ! structural genomics
80684 ! structural genomics
86002 ! structural genomics
89586 ! MJ1084
86273 ! structural genomics
53240 ! this domain is decorated with additional structures; includes N-terminal additional subdomains and extra N-terminal strand
108731 !SQ Q9WZ12 # ! Structural genomics target
110454 ! 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 2134 
110455 ! this domain is also present in several multidomain proteins that are not split in scop yet: scop_sf 56712, scop_sf 56719, scop_sf 56726, scop_sf 56731
106583 !SQ O67859 # ! Structural genomics target
110459 ! 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 2134 
106250 !SQ Q9I3M0 # ! Structural genomics target
52160 ! 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 3214
52163 ! synonym: 50S ribosomal protein L13p, HMAL13
105329 !SQ P29198
52165 ! 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 1423
52168 ! synonym: 50S ribosomal protein L4e, HMAL4, HL6
105321 !SQ P12735
52171 ! 3 layers, a/b/a; parallel beta-sheet of 5 strand, order 21345
62845 ! meta-active conformation
31046 ! thiophosphonate modified
31060 ! bound to the N-terminus of FliM
72751 ! complexed with CheZ
31078 ! bef3-activated
31053 ! naturally-occurring mutant
31081 ! CA-atoms only, mutant protein sequence
107566 !SQ Q56312
104074 !SQ Q52884
31101 ! phosphorylated form
31104 ! also includes a part of the linker region
77721 ! also includes a part of the linker region
77722 ! also includes a part of the linker region
31105 ! C-terminal helix-swapping dimer
104139 !SQ P06628
31112 ! phosphatase resistant mutant
71728 ! mn(2+)-bound form
90944 ! phosphorylated
110464 ! contains extra C-terminal all-alpha subdomain (144-20), 3-helical bundle
105374 !SQ O06143 # ! Structural genomics target
105430 !SQ O06143 # ! Structural genomics target
52198 ! contains coiled coil and small all-alpha subdomains in the C-terminal extension
82344 ! lacks canonical receiver domains features
104850 !SQ Q79PF6 # structured linker 136-176 in swapped dimer
78478 ! CASP5
31130 ! structural genomics
52211 ! contain additional N-terminal strand "0", antiparallel to strand 2
87050 ! alpha-chain only
52219 ! binds FMN
31174 ! apo form
31176 ! apo form
108895 !SQ Q9WZL4 # ! Structural genomics target
107132 !SQ P29476 750-1413
52235 ! binds FAD
110470 ! evolved new enzymatic activity
107003 !SQ P41407 # ! Structural genomics target
106434 !SQ Q8XFP4 # ! Structural genomics target ! complexed with FMN
98969 ! structural genomics; NESG target SPR27
102238 ! Trp repressor binding protein
89590 ! Pfam 03358
89592 ! YhdA gene product
85904 ! structural genomics
106210 !SQ Q07923
105098 !SQ Q9I4D4
109497 !SQ Q9I4D4 5-167 # ! Structural genomics target
104983 !SQ P50618 # ! Structural genomics target
88717 ! active subunit; binds B12
88719 ! inactive subunit
89593 ! TM0446
86628 ! structural genomics
107577 !SQ Q72LC1
52271 ! includes irregular N- and C-terminal extensions
65057 ! heterodimer with alpha2 subunit
65058 ! heterodimer with alpha1 subunit
89595 ! multifunctional enzyme with thioesterase, esterase, protease and lysophospholiase activities
102241 ! putative lipase
52281 ! interdomain linker forms an additional, N-terminal strand
52284 ! this domain is interrupted by the Rossmann-fold domain
52285 ! contains an additional beta-hairpin after the common fold
82347 ! C-terminal binding protein 1; a dehydrogenase
52293 ! has additional C-terminal domain of the ferredoxin fold
63963 ! L-alanine dehydrogenase homologue
91971 ! complexed with dIII component
95102 ! complexed with dIII component
61473 ! complexed with dIII component
52301 ! contains additional secondary structures disguising the superfamily fold
52311 ! class II N-deoxyribosyltransferase
31396 ! complexed with 5-methyl-2'-deoxypseudouridine
102244 ! class I N-deoxyribosyltransferase
52313 ! fold elaborated with additional structures
100739 ! structural genomics
100735 ! structural genomics
63965 ! fold elaborated with additional structures
93539 ! structural genomics
52317 ! conserved positions of the oxyanion hole and catalytic nucleophile; different constituent families contain different additional structures
52318 ! contains a catalytic Cys-His-Glu triad
106332 !SQ P00907
86554 ! structural genomics
102250 ! glutamine amidotransferase of SNO/PDX2 family implicated in pyridoxine biosynthesis
96054 ! structural genomics
105203 !SQ P08398 # interdomain linker (267-286)
108508 !SQ Q5SIA8
108506 !SQ Q5SIA8
108504 !SQ Q5SIA8
106382 !SQ P74881
82351 ! probable non-catalytic branch of the class I GAT family; overall fold is very similar but the active site is not conserved
52325 ! contains a catalytic triad or dyad different from the class I GAT triad
87048 ! structural genomics
89603 ! RNA-binding protein regulatory subunit
105843 !SQ Q99497
89606 ! involved in an early stage of isoprenoid biosynthesis; contains a Cys-Glu putative catalytic dyad
100697 ! structural genomics
87551 ! structural genomics; NESG target ER105
89609 ! contains a buried Cys-His-Asp triad within one subunit
102253 ! contains a buried Cys-His-Glu triad within one subunit
96454 ! structural genomics
96447 ! structural genomics
96445 ! structural genomics
52331 ! probable circular permutation in the common core; contains a catalytic Ser-His-Glu triad
110486 ! overall fold is very similar the class I GAT family but the putative active site has a different structure  
106206 !SQ Q5KY38 # 99% sequence identity (Geobacillus kaustophilus TaxID:1462); ! Structural genomics target
52334 ! 3 layers, a/b/a; parallel beta-sheet of 5 strands, order 32145
52335 ! contains a common phosphate-binding site
106326 !SQ P00968
31509 ! CASP3
62524 ! complexed with phosphoglycolohydroxamic acid
108892 !SQ Q9X0R7 # ! Structural genomics target
106923 !SQ P31335
52342 ! 3 layers, a/b/a; parallel beta-sheet of 5 strands, order 32145
52343 ! binds NADP differently than classical Rossmann-fold ! N-terminal FAD-linked domain contains (6,10) barrel
31548 ! CASP3
104627 !SQ P20070 33-300
52359 ! contains additional 2Fe-2S ferredoxin domain at one of the termini
52362 ! contains 2Fe-2S cluster in the C-terminal extension
107133 !SQ P29476 750-1413
52370 ! contains additional globin domain
52373 ! core: 3 layers, a/b/a ; parallel beta-sheet of 5 strands, order 32145
52375 ! contains a conserved all-alpha subdomain at the C-terminal extension
79966 ! mini-TyrRS; anticodon recognition part is more divergent; secreted cytokine with IL-8-like activity
95528 ! mini-TyrRS
52378 ! overall structure is similar to TyrRS
103891 !SQ P23381 94-471
52382 ! Catalytic domain is very similar to that of GlnRS
102257 ! truncated GluRS and GlnRS homologue lacking the anticodon-binding domain; glutamylates the modified base queuosine (Q) of tRNA-Asp
92377 ! structural genomics
75159 ! similar domain organization to GluRS
105064 !SQ Q9V011 1-606 # C-domain 616-722 is solved separately: 1MKH
83814 ! preliminary structure of ligand-free enzyme; CA-atoms only
82357 ! contains a non-conserved insertion (residues 581-633) that forms a separate subdomain; possible rudiment Zn finger
92564 ! structural genomics 
108829 !SQ Q9WZK0 # ! Structural genomics target
106859 !SQ Q50452
102261 ! TM0379
106603 !SQ Q9WZW1  
106611 !SQ Q9WZW1  
106607 !SQ Q9WZW1  
63976 ! contains C-terminal subdomain similar to one structural repeat of the Creatinase/aminopeptidase family
85036 ! structural genomics
85269 ! structural genomics
85267 ! structural genomics
85275 ! structural genomics
85277 ! structural genomics
85271 ! structural genomics
85273 ! structural genomics
85285 ! structural genomics
100504 ! structural genomics
88488 ! structural genomics
97168 ! truncated form lacking the C-terminal APC kinase-like domain
69455 ! lacks the C-terminal domain
102262 ! lacks the C-terminal domain
52402 ! share similar mode of ligand (Adenosine group) binding ! can be subdivided into two group with closer relationships within each group than between the groups; the first three families form one group whereas the last two families form the other group 
69456 ! Asparagine synthetase B homologue
102263 ! carbapenam synthetase CarA
108714 !SQ Q9X2A1 # ! Structural genomics target
97850 ! structural genomics; NESG target PFR23
82360 ! characterized as tRNA-Ile-lysidine synthetase, TilS
52432 ! alpha/beta heterodimer of homologous subunits; contains additional strands on both edges of the core sheet
81393 ! contains an additional FAD-binding domain of DHS-like fold
106719 !SQ P13804 20-203 ! only the N-terminal domain is ordered in the crystal
81394 ! binds AMP
106720 !SQ P38117
31640 ! structural genomics
69462 ! the nucleotide-binding is not known
66900 ! structural genomics
102266 ! putative universal stress protein
96024 ! structural genomics
107209 !SQ O06153 # ! Structural genomics target
52417 ! 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; Rossmann-like
52424 ! 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; Rossmann-like
52427 ! binds a light-harvesting cofactor
52428 ! cofactor is MHTF
71281 ! complexed with thymine
52429 ! cofactor is HDF
107639 !SQ Q43125 13-497
107637 !SQ Q43125 13-497
75168 ! 3 layers: a/b/a, core: parallel beta-sheet of 5 strands, order 43215
77200 ! structural genomics
73484 ! structural genomics
88722 ! 3 layers, a/b/a; core: parallel beta-sheet of 5 strands, order 32145
86629 ! structural genomics
100530 ! structural genomics
53045 ! contains an alpha-helical arch and additional strand 6 antiparallel to the rest; strand order 321456; similarity to the resolvase-like fold
89622 ! 3 layers: a/b/a, core: parallel beta-sheet of 5 strands, order 21354; topological similarity to a part of the arginase/deacetylase fold
85891 ! structural genomics
102273 ! Rv2465c
89628 ! TM1080
86553 ! structural genomics
75216 ! core: 3 layers: a/b/a, parallel beta-sheet of 5 strands, order 21435; contains a deep trefoil knot
75217 ! known or predicted SAM-dependent methytransferases including the SPOUT 'sequence' superfamily ! all known members have dimeric structures
82371 ! Pfam 02590
80706 ! structural genomics; NESG target ER45
92567 ! structural genomics
100631 ! structural genomics
107160 !SQ Q45601
89629 ! fold and dimerisation mode are similar to those of the YbeA-like family; contains additional C-terminal all-alpha subdomain
93720 ! a TrmD topoisomer that lacks the knot; misfolded inactive structure?  
104092 !SQ P07020
75218 ! contains extra strand (3) in the parallel beta-sheet, order 321546
75219 ! 23S rRNA methyltransferase; proposed gene names are as appear in the original publication (and the PDB entry) 
82376 ! 23S rRNA G2251 2'O-methytransferase
75221 ! contains extra strand (3) in the parallel beta-sheet, order 321546; interrupted by an insert OB-fold domain
89632 ! contains extra strand (3) in the parallel beta-sheet, order 321546; similar dimerisation to the MTH1 domain
100717 ! structural genomics
86394 ! structural genomics
100687 ! structural genomics
52439 ! 3 layers: a/b/a; parallel or mixed beta-sheet of 4 to 6 strands ! possible rudiment form of Rossmann-fold domain
52440 ! precedes the ATP-grasp domain common to all superfamily members, can contain a substrate-binding function
52442 ! subunit of acetyl-CoA and pyruvate carboxylases 
108702 !SQ Q9X0X7 # ! Structural genomics target
52450 ! duplication: CPS large subunit contains two full BC-like lobes: carboxyphosphate and carbamoyl phosphate domains
106328 !SQ P00968
52460 ! circularly permuted version of prokaryotic enzyme
52466 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; Rossmann-like
52467 ! binds cofactor molecules in the opposite direction than classical Rossmann fold
105026 !SQ P49366
104989 !SQ P49366
105060 !SQ P49366
52471 ! lacks strand 3; shares the FAD-binding mode with the pyruvate oxidase domain
52475 ! N-terminal domain is Pyr module, and C-terminal domain is PP module of thiamin diphosphate-binding fold
52476 ! binds FAD
52478 ! rudiment domain with a variant fold, lacks FAD-binding
52484 ! binds NADP, shares with the pyruvate oxidase FAD-binding domain a common ADP-binding mode
91972 ! complexed with dI component
95103 ! complexed with dI component
61474 ! complexed with dI component
63984 ! silent information regulator 2; contains insertion of a rubredoxin-like zinc finger domain
78883 ! complexed with an acetylated p53 peptide, chain B
98569 ! complex with a acetylated substrate peptide,  chain B
95561 ! complexed with histone H4 peptide, chain B
106150 !SQ P53686 1-293
106149 !SQ P53686 1-293
52489 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456
86974 ! complexed with SulA homologue PA3008
105050 !SQ O08378
104986 !SQ O08378
105054 !SQ O08378
107364 !SQ P02554
107362 !SQ P02550
52498 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456
52504 ! octameric hydrolase of unknown specificity
90791 ! structural genomics
109527 !SQ O77166 # 89% sequence identity; Leishmania tarentolae TaxID:5689
63991 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; also contains a C-terminal alpha+beta subdomain
52506 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456
52508 ! formerly DFP DNA/pantothenate metabolism flavoprotein family
52509 ! involved in signal transduction; binds FMN
102300 ! hypothetical protein mds018
63996 ! binds FMN
102301 ! binds FAD
56783 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456
56784 ! contains an insert alpha+beta subdomain; similar overall fold to the Cof family  ! usually contains an insertion (sub)domain after strand 1
69467 ! the insertion subdomain is a beta-hairpin involved into tetramerisation
56785 ! the insertion subdomain is a 4-helical bundle
75173 ! the insertion subdomain is a 4-helical bundle 
74283 ! phosphorylated enzyme
106793 !SQ P77247 # ! Structural genomics target
56789 ! the insertion subdomain is a 4-helical bundle
56790 ! has a lipid phosphatase activity
56792 ! the insertion subdomain is a 4-helical bundle
104889 !SQ O31156
64511 ! the insertion subdomain is a 4-helical bundle
62754 ! Phospho-aspartyl intermediate analogue
73665 ! PI complex
73671 ! complex with substrate
82382 ! the insertion subdomain is a 4-helical bundle; dephosphorylates dUMP and dTMP
102304 ! the insertion subdomain is a rudiment 4-helical bundle
102307 ! the insertion subdomain is a helical hairpin
102310 ! the insertion subdomain is multi-helical
96595 ! structural genomics; NESG target ZR25
82385 ! no insertion subdomains
82388 ! contains an alpha+beta subdomain inserted into a new site after strand 3
77769 ! structural genomics
77632 ! structural genomics; MCSG target APC014
86128 ! structural genomics
91851 ! structural genomics
97622 ! structural genomics; NYSGRC target T1436
102317 ! contains an alpha/beta subdomain inserted after strand 3 (analogous to the Cof family)
102318 ! putative NagD protein
95199 ! structural genomics, 
100832 ! structural genomics
81656 ! interrupted by a large insertion, domain N
106474 !SQ P04191
108581 !SQ P04191
106478 !SQ P04191
75859 ! Structure in the absence of calcium ions
75893 ! Structure in the e2 state
107538 !SQ Q9HIW7 # ! Structural genomics target
110509 ! the insertion subdomain is a 3-stranded beta-sheet; 
106729 !SQ Q9GZU7 76-256
106728 !SQ Q9GZU7 76-256
100949 ! core: 3 layers: a/b/a; parallel or mixed beta-sheet of 6 strands, order 321456
52513 ! share a common phosphate-binding site with the RpiA family
102322 ! TM1154
108707 !SQ Q9X0N8 # ! Structural genomics target
94416 ! structural genomics
75176 ! share a common phosphate-binding site with the NagB-like family; part of sheet is folded upon itself and forms a barrel-like structure like the CoA transferase subunits 
72910 ! structural genomics
78353 ! structural genomics
107898 !SQ Q72J47
107894 !SQ Q72J47
107896 !SQ Q72J47
74657 ! catalytic subunit: similar active site structure to the NagB and RpiA families; mixed beta-sheet of 7 strands, order 4321567; strand 3 is antiparallel to the rest
74656 ! parallel beta-sheet of 7 strands, order 4321567
106724 !SQ Q9X013 # ! Structural genomics target; contains extra N-terminal alpha+beta domain (1-126); beta(3)-alpha(5); 3 layers: b/a/a
109133 !SQ Q06489
106462 !SQ O29877 # AF0370
105858 !SQ O67621 # ! Structural genomics target
105413 !SQ P75430 # ! Structural genomics target
75180 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456
72615 ! structural genomics
63998 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 432156
64004 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 342156
64005 ! the sheet topology is similar to those of the N-terminal domain of phosphoglycerate kinase and carbamate kinase
102323 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213456
102324 ! the sheet topology is similar to those of the Periplasmic binding protein-like I domains
52517 ! 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465
52518 ! there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules ! two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules
88724 ! the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology
88735 ! different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain
88739 ! E1A and E1B fused together in a single-chain protein
88741 ! parent family to TK and PFOR ! heterodimeric protein related to TK; alpha-subunit is the PP module and the N-terminal domain of beta-subunit is the Pyr module
108241 !SQ P21953 52-392
108228 !SQ P21953 52-392
108262 !SQ P21953 52-392
108273 !SQ P21953 52-392
88744 ! chain A is alpha-subunit and chain B is beta-subunit
66174 ! structure determined on its own rather in the complex with E1-alpha
88746 ! domains VI, I and II are arranged in the same way as the TK PP, Pyr and C domains
88749 ! the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology
88760 ! different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain
88764 ! E1A and E1B fused together in a single-chain protein
88766 ! parent family to TK and PFOR ! heterodimeric protein related to TK; alpha-subunit is the PP module and the N-terminal domain of beta-subunit is the Pyr module
108240 !SQ P12694 52-445
108227 !SQ P12694 52-445
108261 !SQ P12694 52-445
108272 !SQ P12694 52-445
88769 ! chain A is alpha-subunit and chain B is beta-subunit
88771 ! domains VI, I and II are arranged in the same way as the TK PP, Pyr and C domains
52539 ! 3 layers: a/b/a, parallel or mixed beta-sheets of variable sizes
52540 ! division into families based on beta-sheet topologies
52541 ! parallel beta-sheet of 5 strands, order 23145
102339 ! Rv1389
52546 ! contains insert 4-helical bundle subdomain, residues 35-145
66449 ! CASP4
104525 !SQ Q97PK6
106817 !SQ P30085
52552 ! contains insert all-alpha subdomain, res. 251-322
103925 !SQ P03176 46-375
52557 ! contains a rudiment "zinc-finger" subdomain, residue 125-161
52558 ! contains a rudiment "zinc-finger" subdomain, residue 147-176
52559 ! contains a rudiment "zinc-finger" subdomain, residue 131-168
52560 ! contains a rudiment "zinc-finger" subdomain, residue 122-156
31914 ! contains a rudiment "zinc-finger" subdomain, residue 128-158
52562 ! contains a zinc-finger subdomain, residues 126-160
102341 ! contains a zinc-finger subdomain, residues 126-160
102342 ! contains a zinc-finger subdomain, residues 126-160
102343 ! contains no zinc finger-like insertion
100702 ! structural genomics
100690 ! structural genomics
100783 ! structural genomics
99119 ! structural genomics; NESG target ER57
102344 ! TT1252
99328 ! structural genomics
106208 !SQ P54288 234-451
106212 !SQ P54288 234-451
106359 !SQ P54288
106380 !SQ P54288
108917 !SQ P54287 38-362
108911 !SQ P54287 38-362
108921 !SQ P54287 38-362; beta4 isoform with odd numbering
52566 ! similar to the nucleotide/nucleoside kinases but acts on different substrate
100755 ! structural genomics
52569 ! similar to the nucleotide/nucleoside kinases but acts on different substrate
75195 ! similar to the nucleotide/nucleoside kinases
82395 ! similar to the nucleotide/nucleoside kinases; extra N- and C-terminal structures
52575 ! Pfam 00685 ! similar to the nucleotide/nucleoside kinases but transfer sulphate group
102349 ! cytosolic enzyme
102351 ! cytosolic enzyme
108668 !SQ O35310 48-311
106821 !SQ P84151
106686 !SQ Q9Y663 139-406 # isoform 3A1; 100% sequence identity to isoform 3B1 domain (SQ Q9Y662 133-390)
106688 !SQ Q9Y663 139-406 # isoform 3A1; 100% sequence identity to isoform 3B1 domain (SQ Q9Y662 133-390)
52587 ! has a circularly permuted fold compared to the phosphoribulokinase fold
105885 !SQ P15044
102356 ! close structural similarity to PanK
102358 ! structural similarity to PanK
98132 ! structural genomics
52590 ! bifunctional enzyme
52592 ! core: mixed beta-sheet of 6 strands, order 231456; strand 2 is antiparallel to the rest
72179 ! complex with bry2 RBD
32002 ! rac1
98103 ! alternative splicing variant of rac1
98100 ! alternative splicing variant of rac1
32004 ! rac1 in complex with the GAP domain of ExoS
32005 ! rac1 in complex with the GAP domain of SptP
32006 ! rac2 in complex with RhoGDI (chain A)
32007 ! rac1
61684 ! rac1 in complex with arfaptin
61731 ! rac1 in complex with arfaptin
61720 ! rac1 in complex with arfaptin
61038 ! rac1 in complex with RhoGD
88378 ! complexed with the Sec5 domain Ral-binding domain
61570 ! complexed to RCC1
109515 !SQ P61586 2-181
97244 ! complexed with a sec7 domain
97317 ! complexed with a sec7 domain
97247 ! complexed with a sec7 domain
98750 ! complexed with a sec7 domain
72914 ! complexed with GMP-PDE delta
72912 ! complexed with GMP-PDE delta
72916 ! complexed with GMP-PDE delta
78491 ! complexed with sec23
52623 ! common fold is interrupted with an all-alpha domain
106051 !SQ P10824
106050 !SQ P10824
72627 ! bound to the goloco motif of rgs14, chains B and D
32096 ! species chimera
32104 ! species chimera
64737 ! one domain only
103902 !SQ P02990
64732 ! one domain only
52631 ! eukaryotic and archaeal homologue of EF-Tu
105683 !SQ P35021
52633 ! has internal nucleotide exchange factor built in as an insertion subdomain
52634 ! residues 160-252 comprise insertion subdomain
107618 !SQ P32324
75204 ! includes rubredoxin-like zinc finger insert domain, res. 56-83
98304 ! structural genomics
97384 ! low-resolution NMR structure
82406 ! member of EngA subfamily of GTPases; contains two G domains
102368 ! TT1381
82410 ! Member of the Obg family of GTPases; contains an alpha-hairpin insert subdomain
89666 ! HI0393
84140 ! structural genomics
88293 ! structural genomics
106048 !SQ P38424
106024 !SQ P38424
106057 !SQ P38424
89669 ! naturally occurring circular permutation of G-domain; includes C-terminal all-alpha subdomain
88294 ! structural genomics
69488 ! the family common core is decorated with large insertions
104805 !SQ O74718
104808 !SQ O74718
104811 !SQ O74718
105371 !SQ P24408
109415 !SQ P51151 2-175 # 100% sequence identity do the dog protein (SQ P24408 2-175)
108609 !SQ P09527
108599 !SQ P09527
108598 !SQ P09527
108621 !SQ P09527
110542 ! circularly permuted G-domain similar to B. sutilis YlqF; distinct extra C-terminal all-alpha subdomain 
107556 !SQ Q9X242 # TM1717
107918 !SQ P01123
107201 !SQ Q9QZ85 # ! G domain is inserted in all-alpha domain (14-68,252-415)
107195 !SQ Q9QZ85 # ! G domain is inserted in all-alpha domain (14-68,252-415)
107223 !SQ Q9QZ85 # ! G domain is inserted in all-alpha domain (14-68,252-415)
107202 !SQ Q9QZ85 # ! G domain is inserted in all-alpha domain (14-68,252-415)
107200 !SQ Q9QZ85 # ! G domain is inserted in all-alpha domain (14-68,252-415)
52642 ! common fold is interrupted with some all-alpha subdomains
105954 !SQ P24733 6-837
105264 !SQ P24733 3-836
75206 ! lacks the SH3-like insert domain
108592 !SQ P33173 3-355
108595 !SQ P33173 3-355
108593 !SQ P33173 3-355
108594 !SQ P33173 3-355
52649 ! contains coiled-coil neck
52651 ! kinesin-like protein
105438 !SQ Q41460 884-1252
52652 ! core: parallel beta-sheet of 7 strands; order 3241567
52655 ! common fold is interrupted by an all-alpha subdomain, residues 100-200
52659 ! modified P-loop; there are many insertions in the common fold
78456 ! chemically crosslinked structure
108890 !SQ Q9WZ40 # ! Structural genomics target
52668 ! Duplication: consists of two domains of this fold arranged as the NIP subunits in the dimer
89671 ! homologue of the cobalamin biosynthesis protein CobW
85741 ! CASP5 ! structural genomics
89673 ! forms segment-swapped dimer
105204 !SQ P08398 # interdomain linker (267-286)
108509 !SQ Q5SIA8
108507 !SQ Q5SIA8
108505 !SQ Q5SIA8
52670 ! core: mixed beta-sheet of 8 strands, order 32451678; strand 7 is antiparallel to the rest
52671 ! C-terminal domain is alpha+beta
107743 !SQ P03017 
107745 !SQ P03017 
107747 !SQ P03017 
52719 ! type II/IV secretion system protein; includes N-terminal alpha+beta domain of a profilin-like topology
32431 ! structural genomics
102375 ! type II/IV secretion system protein; overall structure is similar to HP0525
79772 ! complex with BRCA2 BRC4 repeat peptide
106187 !SQ P25454 81-395
106419 !SQ O73948
108997 !SQ P19483
109016 !SQ P19483
109006 !SQ P00829
109025 !SQ P00829
52682 ! lacks the last strand 8
52684 ! lacks the two last strands
108388 !SQ Q14565
110558 ! duplication: contains two copies of this domain
106849 !SQ Q79PF4 14-497
89678 ! homologous to RecA but lacks its P-loop motif; the fold is C-terminally truncated; 5-stranded parallel beta-sheet, order: 15423
86977 ! complexed with FtsZ
52686 ! there are two additional subdomains inserted into the central core that has a RecA-like topology
32372 ! CASP4
89685 ! a low-resolution structure of the E. coli MsbA in an open conformation is also available </i>(<a href="../search.cgi?sccs=f.35.1.1">f.35.1.1</a>)<i>
88058 ! structure in a closed conformation
32373 ! N- and C-terminal subdomains only; the middle coiled coil domain is deleted
32375 ! N- and C-terminal subdomains only; the middle coiled coil domain is deleted
99859 ! N- and C-terminal subdomains only; the middle coiled coil domain is deleted
62417 ! N- and C-terminal subdomains; include a small fragment of the middle coiled coil domain
32381 ! N- and C-terminal subdomains only; the middle coiled coil domain is deleted
32382 ! N-terminal (sub)domain only; in the absence of the C-terminal domain complementing the central core structure, the P-loop region folds in a helix-loop-helix structure
32384 ! CASP4
109223 !SQ P23909 2-800
105541 !SQ Q8U2E3 # ! Structural genomics target
81268 ! duplication: tandem repeat of two RecA-like (AAA) domains
52701 ! each AAA domain contains an all-alpha insert subdomain
52704 ! homologous to eIF4a and UrvB
95513 ! N-terminal domain only
100576 ! N-terminal domain only
52706 ! homologous to UvrB
32409 ! C-terminal domain
32410 ! N-terminal AAA domain; P-loop is empty and in a non-canonical conformation
32411 ! N-terminal AAA domain; P-loop is empty and in a non-canonical conformation
52708 ! contains large insertions in the first AAA domain
106458 !SQ P56981
82414 ! a pre-protein crosslinking domain inserted in the first AAA domain
106837 !SQ P28366
106833 !SQ P28366
106577 !SQ Q13838 45-251; 261-428 # separate coverage for the N-terminal AAA domain 1T6N and the C-terminal AAA domain 1T5I 
106450 !SQ Q13838 45-251; 261-428 # separate coverage for the N-terminal AAA domain 1T6N and the C-terminal AAA domain 1T5I 
81269 ! fold is similar to that of RecA, but lacks the last two strands, followed by a family-specific Arg-finger domain
52711 ! contains additional alpha-helical domain after the family specific domains
85784 ! AAA+ domain only; nucleotide-bound form
85786 ! AAA+ domain only; nucleotide-free form
63234 ! N-terminal subdomain only
64035 ! contains additional alpha-helical domain after the family specific domains
82416 ! contains TrpR-like DNA-binding domain after the family specific domains
52713 ! contains "winged helix" DNA-binding domain after the family specific domains
92320 ! inactive state
92334 ! AAA+ domain only in the active state 
52715 ! contains "winged helix" DNA-binding domain after the family specific domains
59184 ! D1 domain from the N-D1 fragment 
93803 ! complete low resolution structure
98455 ! D1 domain from the N-D1 fragment 
82418 ! ATP-dependent protease
52721 ! ATPase subunit of ATP-dependent protease
102391 ! ATPase subunit of ATP-dependent protease
96651 ! C-terminal all-alpha subdomain only
82421 ! duplication: two AAA+ modules; the first module is structurally similar to the CDC6 module whereas the second module to the HslU module
104820 !SQ Q83LR6
75211 ! ATPase subunit of ATP-dependent protease; similar domain organization to ClpA
71631 ! N-terminal subdomain only
60376 ! CASP4
107546 !SQ P03132 225-490
105383 !SQ P03132 225-490
106082 !SQ P38630 295-696 # helical segment (667-696) together with unassigned C-terminal sequence forms an all-alpha subdomain  
106084 !SQ P40339
106086 !SQ P38629
106088 !SQ P40348
106090 !SQ P38251
107333 !SQ P06789 428-629 # structure of the origin-binding domain (210-354) is also known, 1r9w (scop_sp 103119)
52724 ! duplication: consists of two similar domains, one binds NTP and the other binds RNA; also contains an all-alpha subdomain in the C-terminal extension
71821 ! an engineered arginine-rich subdomain 2
87137 ! an engineered arginine-rich subdomain 2
69497 ! contains a mobile insertion of LEM/SAP-like HeH motif, residues 354-423
65258 ! less ordered regions are modeled as poly-ALA
102396 ! contains extra N-terminal alpha+beta subdomain
75213 ! mixed beta-sheet; order 234156(0), strands 2 and 6 are antiparallel to the rest
71085 ! complexed with ADP and magnesium
70139 ! structural genomics ! CASP4
52727 ! 3 layers: a/b/a, parallel beta-sheet of 6 strands, order 324156
102399 ! 3 layers, a/b/a; parallel beta-sheet of 7 strands, order 7165243
102400 ! structural similarity and possible evolutionary relationship to the AAA domain; lacks the P-loop motif
52732 ! 3 layers: a/b/a, parallel beta-sheet of 7 strands, order 3214567
102404 ! 3 layers: a/b/a, parallel beta-sheet of 7 strands, order 4321567
102406 ! Pfam 03641
102408 ! structural genomics; NESG target VT76
99115 ! structural genomics; NYSGRC target T833
52737 ! 3 layers: a/b/a, parallel beta-sheet of 7 strands, order 3421567
52742 ! 3 layers: a/b/a, parallel beta-sheet of 7 strands, order 2314567; left-handed crossover connection between strands 2 & 3
32486 ! propeptide complex
107067 !SQ P29600
32532 ! CASP1
104083 !SQ P06873
104082 !SQ P06873
109409 !SQ Q93UV9 207-640
109411 !SQ Q93UV9 207-640
109413 !SQ Q93UV9 207-640
52764 ! elaborated with additional structures
32556 ! CASP4
106246 !SQ Q8RR56
106244 !SQ Q8RR56 
106248 !SQ Q8RR56
105806 !SQ Q8GB88
110580 ! core: 3 layers, a/b/a; parallel beta-sheet of 7 strands, order 2134756
108675 !SQ Q9X1H5 # ! Structural genomics target
52767 ! 3 layers: a/b/a, parallel beta-sheet of 8 strands, order 21387456
109451 !SQ Q9RZ04 # DRA0149
109457 !SQ Q9RZ04 # DRA0149
109445 !SQ Q9RZ04 # DRA0149
106544 !SQ Q9BY41
106553 !SQ Q9BY41
108661 !SQ Q9BY41
106554 !SQ Q9BY41
109084 !SQ Q9BY41 13-375
102413 ! 3 layers: a/b/a; parallel beta-sheet of 8 strands, order 54321678
64042 ! beta(2)-(alpha-beta)2-beta; 2 layers, a/b; mixed beta-sheet of 5 strands, order 12345; strands 1 & 5 are antiparallel to the rest
69499 ! beta(2)-(alpha-beta)2-beta(3); 3 layers, a/b/b; some topological similarity to the N-terminal domain of MinC
69500 ! active form is a dimer
69502 ! formerly hypothetical protein YihZ
89696 ! YihZ homologue HI0670
84130 ! structural genomics
106755 !SQ P84066 # ! Structural genomics target
52776 ! core: 2 layers, a/b; mixed beta-sheet of 6 strands, order 324561; strands 3 & 6 are antiparallel to the rest
52778 ! trimeric enzymes with the active sites being located in between subunits
104492 !SQ P00483
104120 !SQ P00483
82424 ! monomeric enzyme containing tandem repeat of two CAT subunit-like domains
82425 ! relative spatial position of the domains is similar to the monomers in CAT trimer
106628 !SQ P47934
106630 !SQ P47934
106634 !SQ P47934
104544 !SQ P32738
75229 ! condensation domain (Pfam 00668) ! functional domain of multifunctional enzyme containing tandem repeat of two CAT subunit-like domains
75230 ! relative spatial position of the domains is similar to the monomers in CAT trimer
104593 !SQ P96208
52787 ! 3 layers: a/b/a; parallel beta-sheet of 4 strands, order 2134
52788 ! share the common active site structure with the family II
104084 !SQ O00810
69504 ! also has a phosphotyrosine phosphatase activity
105116 !SQ P30330
105115 !SQ P30330
52796 ! of the phosphoenol-pyruvate dependent phosphotransferase system
108689 !SQ P00550 375-471
52798 ! core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1423
52799 ! share with the family I the common active site structure with a circularly permuted topology
66392 ! complexed with phosphopeptide
89698 ! duplication: consists of two structurally similar domains with the catalytic site being in the C-terminal domain
52805 ! has an extension to the beta-sheet of 3 antiparallel strands before strand 4
106022 !SQ P18031 2-299
106403 !SQ P18031 1-298
106402 !SQ P18031 1-298
32673 ! cysteinyl-phosphate intermediate
106422 !SQ P18031 1-298
52808 ! receptor protein tyrosine phosphatase mu, domain 1
52809 ! receptor protein tyrosine phosphatase alpha, domain 1
32684 ! contains tandem repeat of two SH2 domains in the N-terminal region
59949 ! complex with an in vitro peptide substrate py469 derived from shps-1, chain B
75233 ! non-receptor type 2
96608 ! complexed with a phosphotyrosyl mimetic-containing hexapeptide, chains C, D, E and F
52815 ! duplication: tandem repeat of the phosphatase domain
93895 ! D2 domain
102422 ! common fold is decorated with additional structures
52820 ! 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32451
52821 ! the active site structure is similar to those of the families I and II protein phosphatases; the topology can be related by a different circular permutation to the family I topology
106357 !SQ Q8GY31
69510 ! single-domain rhodanese
107198 !SQ Q39129 # ! Structural genomics target
52827 ! duplication: consists of two domains of this fold
32706 ! complex with lipoate
107763 !SQ Q5SJI0
52832 ! core: 3 layers, a/b/a; mixed beta-sheet of 4 strands, order 4312; strand 3 is antiparallel to the rest
32724 ! active-site variant
32729 ! CA-atoms only
92742 ! insertion mutant
107076 !SQ P00581
107088 !SQ P00581
107065 !SQ P00581
107081 !SQ P00581
105708 !SQ P00274
105705 !SQ P00274
105686 !SQ P00274
105696 !SQ P00274
105689 !SQ P00274
105702 !SQ P00274
52837 ! thioredoxin H
105068 !SQ P80579
32737 ! short form
32738 ! long form
78745 ! human-escherichia coli thioredoxin chimera
99039 ! structural genomics
109586 !SQ P29448 # ! Structural genomics target
32768 ! mixed disulfide bond with ribonucleotide reductase b1 fragment
89701 ! HI0572
97197 ! segment-swapped dimer
64054 ! single-domain PDI
102433 ! behaves as true thioredoxin; probable MJ0307 ortholog
98820 ! disulfide-linked complex with the N-terminal domain
105465 !SQ O95881 23-172 # ! Structural genomics target
107309 !SQ Q8P6W3
52849 ! duplication: contains two tandem repeats of this fold
32776 ! C-terminal domain
32774 ! C-terminal domain
32775 ! N-terminal domain
89702 ! glutaredoxin-like protein
52855 ! duplication: contains three tandem repeats of this fold
100953 ! contains an all-alpha subdomain insertion
100954 ! the insert subdomain is a 4-helical bundle
99645 ! circularly permuted cpdsba_q100t99
100956 ! TcpG, periplasmic enzyme required for the maturation of secreted virulence factors
102437 ! contains larger and less compact insertion in the common fold than DsbA 
32954 ! CA-atoms only
32950 ! CA-atoms only
83159 ! chimeric isozyme
104181 !SQ P08263
104185 !SQ P08263
104173 !SQ P08263
108004 !SQ P08263
104177 !SQ P08263
107758 !SQ P08515
52875 ! synonym: hematopoietic prostaglandin D synthase
89705 ! synonym: hematopoietic prostaglandin D synthase
107396 !SQ Q9NJQ6 # Fragment
64058 ! maleylacetoacetate isomerase
81366 ! formerly a part of class theta enzymes
102442 ! cannot be assigned to any of the known GST classes
64060 ! similar to class zeta enzymes
52886 ! similar to class phi enzymes
69514 ! similar to class theta enzymes; the N-domain undergoes a redox-controlled structural transition
97595 ! oxidized form; adopts different all-alpha dimeric fold
52889 ! the transducin beta subunit-binding subdomain is an irregular array of helices in the N-terminal extension
102446 ! related to glutaredoxin 1 (GRX1) but lacks both conserved cysteine residues
106279 !SQ Q91VW3
52898 ! elaborated common fold
84259 ! complexed with DsbD-alpha
106341 !SQ P45111 20-228
108373 !SQ P77202
108369 !SQ P77202
52902 ! contains many insertions in the common fold
61784 ! complexed with glutathionylspermidine
52907 ! heme-binding protein 23, HBP23
89709 ! HI0572
88284 ! structural genomics
102454 ! HI0751
96254 ! structural genomics; NYSGRC target T1429
108453 !SQ Q9D0Y4  # ! Structural genomics target
109471 !SQ Q9BRA2
33083 ! CASP3
102461 ! 3 layers: a/b/a; mixed beta-sheet of 4 strands, order 2143, strand 4 is antiparallel to the rest
102463 ! UPF0099: Pfam01981
102464 ! Peptidyl-tRNA hydrolase; involved in apoptosis
52921 ! 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 13245, strand 1 is antiparallel to the rest
52924 ! two N-terminal domains are PP and Pyr modules of thiamin-binding fold
75239 ! E1A and E1B fused together in a single-chain protein
108242 !SQ P21953 52-392
108229 !SQ P21953 52-392
108263 !SQ P21953 52-392
108274 !SQ P21953 52-392
52934 ! 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32145, strand 5 is antiparallel to the rest
110616 ! probable flavoenzyme, binds FMN; the phosphoribityl group binds in the equivalent site to the binding site of the PK allosteric regulator FBP   
106432 !SQ O27711 # ! Structural genomics target
52943 ! contains an antiparallel coiled coil formed by N- and C-terminal extensions to the common fold
109007 !SQ P05631
109026 !SQ P05631
60756 ! core domain is disordered; only coiled coil part is visible
33159 ! core domain is disordered; only coiled coil part is visible
33160 ! core domain is disordered; only coiled coil part is visible
33161 ! core domain is disordered; only coiled coil part is visible
33163 ! core domain is disordered; only coiled coil part is visible
60777 ! core domain is disordered; only coiled coil part is visible
33162 ! core domain is disordered; only coiled coil part is visible
87033 ! core domain is disordered; only coiled coil part is visible
33164 ! core domain is disordered; only coiled coil part is visible
33165 ! partly disordered
59999 ! complexed to the epsilon subunit; the coiled-coil part is disordered
52953 ! 3 layers: a/b/a; mixed beta-sheet of five strands, order 21345; strand 4 is antiparallel to the rest
33205 ! a truncated form of the enzyme
33207 ! a truncated form of the enzyme
33209 ! a truncated form of the enzyme
72819 ! a truncated form of the enzyme
108435 !SQ Q9HCD5 197-313 # ! Structural genomics target
52969 ! contains additional structures in the C-terminal extension
52972 ! elaborated with additional structures inserted in the common fold
52975 ! MJ0226
33224 ! structural genomics
102470 ! PH1917
100482 ! structural genomics
75242 ! putative ribosomal protein
33228 ! structural genomics
107579 !SQ P39432
64075 ! core: 3 layers, b+a/b/a ; the central mixed sheet of 5 strands: order 21534; strand 2 is antiparallel to the rest
52979 ! core: 3 layers, a/b/a; mixed beta-sheet of 5 strands, order 12345; strands 2 &, in some families, 5 are antiparallel to the rest
33299 ! free enzyme
102472 ! local sequence similarity to BglII
62127 ! complexed with 17mer DNA
107380 !SQ P44413
109600 !SQ P17743
109596 !SQ P17743
86849 ! bound to the reaction product site
53027 ! a catalytic component of the tn7 transposition system
53030 ! forms dimer by swapping the common core elements
33339 ! CASP4
105401 !SQ P11405
102477 ! duplication: one subunit consists of two tetrameric tRNA splicing endonuclease subunit-like repeats
53040 ! Core: 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 21345; strand 5 is antiparallel to the rest
33350 ! CA-atoms only
106617 !SQ P61517
53060 ! duplication: consists of two similar domains
53061 ! 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 21345; strand 5 is antiparallel to the rest
53062 ! active dimer is formed by strand 5 swapping
53066 ! 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32145; strand 2 is antiparallel to the rest
53067 ! duplication contains two domains of this fold
106394 !SQ 02568
105923 !SQ P02568
104927 !SQ P02568
82437 ! sequence identical to the rabbit actin
33444 ! dictyostelium/tetrahymena chimera
33446 ! dictyostelium/tetrahymena chimera
69528 ! part of Arp2/3 complex
69530 ! part of Arp2/3 complex
68307 ! the second half only
33454 ! CASP4
82441 ! includes the insert and linker domains
102479 ! Hexokinase D
53086 ! further duplication: consists of two very similar lobes
104473 !SQ P46880 
106559 !SQ O67040
106563 !SQ O67040
110633 ! ubiquitous cytoplasmic protein; annotated as Glycoprotease (Peptidase_M22 family) on the basis of one member's known activity outside the cell
104005 !SQ P76256
109465 !SQ Q7WT42 11-263 # Fragment
53096 ! synonym: Xaa-Pro dipeptidase, prolidase
53098 ! consists of one domain of this fold
107765 !SQ O59351
33589 ! CA-atoms only
105205 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
105214 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
105211 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
105217 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
104676 !SQ P03366 186-725 # chain A coverage; chain B coverage: 156-584
107347 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595
105208 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
81078 ! RNase H domain only
53116 ! contains additional all-alpha subdomains in both N- and C-terminal regions
79494 ! complexed with resolved outside end DNA
79485 ! complexed with transposon end DNA
79493 ! 20mer outside end 2 mn complex
79301 ! complexed with Me DNA
53119 ! part of Klenow fragment, KF
107664 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107654 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107658 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107660 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107662 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107755 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107753 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107074 !SQ P00581
107086 !SQ P00581
107063 !SQ P00581
107079 !SQ P00581
105706 !SQ P00581
105703 !SQ P00581
105684 !SQ P00581
105694 !SQ P00581
105687 !SQ P00581
105700 !SQ P00581
53125 ! elaborated with additional structures and the N-terminal subdomain
102482 ! DNA polymerase II, additional N-terminal subdomain has an OB-fold with a ferredoxin-like fold insertion
53126 ! additional N-terminal subdomain contains rudimental OB-fold
33714 ! exonuclease domain only
33716 ! exonuclease domain only
53127 ! additional N-terminal subdomain contains rudimental OB-fold and rudimental ferredoxin-like fold
53128 ! additional N-terminal subdomain contains rudimental OB-fold but complete ferredoxin-like fold
53129 ! additional N-terminal subdomain contains rudimental OB-fold but complete ferredoxin-like fold
53130 ! additional N-terminal subdomain contains rudimental OB-fold but complete ferredoxin-like fold
53131 ! additional N-terminal subdomain contains rudimental OB-fold but complete ferredoxin-like fold
53132 ! also includes an alpha+beta domain with SH3-like like motif and non-globular C-terminal all-alpha region
89720 ! HI1715
84135 ! CASP4 ! structural genomics
102483 ! forms a ring-shaped hexamer; function unknown
100844 ! structural genomics
53135 ! Holliday junction-specific endonuclease
92166 ! structural genomics
91979 ! structural genomics
93607 ! structural genomics
100713 ! structural genomics
90706 ! N-terminal fragment lacking the C-terminal helix
110641 ! includes the middle domain
107540 !SQ Q8U3D2 # consists of 4 domains: N-terminal (1-152,269-323) [two ferredoxin-like folds inserted one in the other]; PAZ (153-268); middle (324-547) [alpha/beta, 3layers a/b/a; parallel 4-stranded beta-sheet, order 2134]; PIWI (548-770)
105333 !SQ P14123
33739 ! structural genomics
80762 ! structural genomics ! CASP5
104890 !SQ Q9X116 # ! Structural genomics target
102496 ! capable of binding the iron molybdenum cofactor, FeMo-co
33741 ! CASP4
109224 !SQ P23909 2-800
106334 !SQ P16455 6-176
106338 !SQ P16455 6-176
53162 ! core: 3 layers, a/b/a ; mixed sheet of 5 strands: order 21354; strand 4 is antiparallel to the rest; contains crossover loops
53163 ! the HybD fold coincides with the consensus core structure
64095 ! elaborated with the N-terminal alpha+beta subdomain and the insertion all-alpha dimerisation subdomain
53167 ! complex architecture; contains mixed beta-sheet of 8 strands, order 23415867, strands 3, 6 & 7 are antiparallel to the rest; and barrel, closed; n=5, S=8
104142 !SQ P00491
108349 !SQ P55859
100711 ! structural genomics
100679 ! structural genomics
53177 ! also includes the PDB entry </i>(<a href="../pdb.cgi?pdb=1rxs">1rxs</a>)<i> where protein chains are designated by both upper case and lower case letters creating problems with its processing and presentation in SCOP
105426 !SQ Q13126
105427 !SQ Q13126
110645 ! contains extra N-terminal oligomerisation (sub)domain (8-153)
106684 !SQ P15272
106678 !SQ P15272
106694 !SQ P15272
106700 !SQ P15272
53187 ! core: mixed beta-sheet of 8 strands, order 12435867; strands 2, 6 & 7 are antiparallel to the rest
78604 ! high resolution structure
33814 ! truncated beta form with two zinc ions in the active site
33822 ! zymogen
33824 ! procarboxypeptidase A2
33825 ! zymogen
73081 ! zymogen
33826 ! CA-atoms only
53206 ! synonym: Vibrio proteolyticus
107430 !SQ Q01693
82450 ! unspecific amino dipeptidase
100779 ! structural genomics 
100622 ! structural genomics
96045 ! catalytic domain only made of the two separate chains
102513 ! contains insert beta-barrel domain
100670 ! structural genomics 
102515 ! contains insert beta-barrel domain
100695 ! structural genomics 
53213 ! circular permutation of the common fold, most similar to the PNP fold
53217 ! 3 layers: a/b/a; mixed beta-sheet of 5 strands; order: 21354, strand 5 is antiparallel to the rest; permutation of the Phosphorylase/hydrolase-like fold
104782 !SQ P30746
64102 ! the human neuroreceptor anchoring protein
69537 ! gephyrin homologue
108059 !SQ Q39054 464-623
108058 !SQ Q39054 464-623
106353 !SQ Q03555 350-768 # structure on the N-terminal domain (1-201) is also known (1ihc; scop_sp 64101)
110649 ! 3 layers: a/b/a; mixed beta-sheet of five strands, order 21345; strand 1 is antiparallel to the rest 
108640 !SQ Q9X1J4 # ! Structural genomics target
102521 ! 3 layers: a/b/a; mixed beta-sheet of 6 strands; order: 213546, strand 5 is antiparallel to the rest; topological similarity to the MogA-like family fold
52128 ! 3 layers, a/b/a; core: mixed beta-sheet of 6 strands, order 213456, strand 6 is antiparallel to the rest
52129 ! mature protein may be composed of two chains folded in a single domain
61604 ! complexed to xiap-bir2
105416 !SQ P29466
105417 !SQ P29466
105415 !SQ P29466
59597 ! complex with acetyl-Asp-Glu-Val-Asp-CHO
61722 ! Complexed to the xiap linker (chains C and D)
66030 ! complexed to the xiap-bir2 fragment (chains E and F)
68691 ! complexed to the xiap-bir2 fragment (chains C and D)
105557 !SQ P55210 57-303
105555 !SQ P55210 57-303
61686 ! complexed to p35
86294 ! complexed to the xiap-bir3
52137 ! contains extra N-terminal alpha/beta subdomain
52138 ! Arginine-specific cysteine proteinase
52948 ! 3 layers: a/b/a; mixed beta-sheet of 6 strands, order 165243, strand 3 is antiparallel to the rest
75241 ! involved in Xer site-specific recombination; probable DNA-binding domain
89724 ! found in different proteins, including macro-H2a histone and the Appr-1"-p processing enzyme
89725 ! contains extra N-terminal strand
100703 ! structural genomics
98957 ! structural genomics; NESG target ER58
110654 ! contains structural variations at both termini
103858 !SQ Q04299
53243 ! 3 layers: a/b/a; mixed beta-sheet of 6 strands, order 126345; strand 1 is antiparallel to the rest
82453 ! TM0231
77095 ! structural genomics
102532 ! TM0166
92530 ! structural genomics
53253 ! core: 3 layers, a/b/a; mixed beta-sheet of 6 strands, order 324156; strand 5 is antiparallel to the rest
106668 !SQ P07738
104620 !SQ O00092
105674 !SQ O00092 30-464
105672 !SQ O00092 30-464
105673 !SQ O00092 30-464
53268 ! bifunctional enzyme
53270 ! core: 3 layers, a/b/a; mixed beta-sheet of 6 strands, order 321456; strand 3 is antiparallel to the rest
104396 !SQ Q9NJI5
104054 !SQ Q27796
104058 !SQ Q27796
104052 !SQ Q27796
77654 ! ternary complex
102538 ! TM0721
92512 ! structural genomics
109612 ! bifunctional protein; contains the uracil PRTase and Pyr RNA-binding activities
102537 ! TT1027
99357 ! structural genomics
103871 !SQ P41007
53296 ! duplication: consists of two domains of this fold
53299 ! core: 3 layers, a/b/a; mixed beta-sheet of 6 strands, order 321456; strand 3 is antiparallel to the rest
109570 !SQ P20701 153-334
109568 !SQ P20701 153-334
34128 ! complexed with lovastatin
79410 ! complex with ICAM-1
98959 ! complexed with platelet glycoprotein Ib alpha chain
99284 ! complexed with bitiscetin
71234 ! complexed with botrocetin
74361 ! complexed with glycoprotein Ib alpha domain
84966 ! complexed with humanized neutralizing Fab
108408 !SQ P17301 172-364
82456 ! Leukocyte adhesion glycoprotein P150,95 alpha chain
102543 ! Anthrax toxin receptor 2
106557 !SQ P58335 41-210
94509 ! complexed with a snare peptide
94499 ! complexed with a snare peptide
94504 ! complexed with a snare peptide
53322 ! 3 layers: a/b/a; mixed beta-sheet of 6 strands, order 231456; strand 3 is antiparallel to the rest
53325 ! also includes linker domain IV
102545 ! 3 layers: a/b/a; mixed beta-sheet of 6 strands, order 251634; strand 6 is antiparallel to the rest
52150 ! core: 3 layers, a/b/a; mixed beta-sheet of 6 strands, order 432156; strand 4 is antiparallel to the rest
52152 ! the superfamily common core covers almost all of the family fold
53645 ! common core is decorated with many additional structures; mixed beta-sheet of 9 strands, order 654321798; strands 4, 6 and 8 are antiparallel to the rest
89729 ! plant proteins; structurally and functionally related to animal cytosolic phospholipase A2
89732 ! core: 3 layers, a/b/a; mixed sheet of 7 strands, order 1237456; strands 1, 6 and 7 are antiparallel to the rest
89733 ! topological similarity to the domain 2 of TM1585
89734 ! type II malate/L-lactate dehydrogenase; Pfam 02615
86390 ! structural genomics
98363 ! structural genomics
53327 ! 3 layers: a/b/a; mixed beta-sheet of 7 strands, order 3214567; strand 6 is antiparallel to the rest
53334 ! core: 3 layers, a/b/a; mixed beta-sheet of 7 strands, order 3214576; strand 7 is antiparallel to the rest
102554 ! evolved a different function; binds SAM and SAH
107376 !SQ Q06528
107372 !SQ Q06528
90507 ! structural genomics
34181 ! structural genomics
89737 ! AF2087
86149 ! structural genomics; complex with Nop5p (AF2088)
90506 ! structural genomics
95063 ! structural genomics
102558 ! 23S rRNA N1-G745 methyltransferase
94379 ! structural genomics; NESG target ER19
53363 ! contains additional all-alpha C-terminal domain (res.181-248)
69555 ! overall structure is very similar to those of Ermc' and Ermam
104658 !SQ P06992
89741 ! structurally and functionally similar to VP39
104817 !SQ P12823 2495-2756
102560 ! mRNA capping enzyme
34182 ! structural genomics
69546 ! structural genomics
66213 ! CASP4
104829 !SQ Q14749
104856 !SQ Q9QXF8
104864 !SQ Q9QXF8
80579 ! structural genomics ! CASP5
102570 ! involved in the regulation of protein phosphatase 2a activity 
82474 ! MTH146
77681 ! structural genomics
77674 ! structural genomics
77611 ! structural genomics
77670 ! structural genomics
82476 ! contains an inserted alpha helical subdomain
78719 ! CASP5
89744 ! contains an N-terminal alpha helical subdomain; res. 13-84
105528 !SQ Q9WYV8 # ! Structural genomics target
106392 !SQ P37186
89747 ! a non-SET domain nucleosomal histone methyltransferase
107628 !SQ Q04089 176-581
69551 ! a template structure of protein arginine methyltransferase
53351 ! lacks the last two strands of the common fold replaced with a beta-sandwich oligomerisation subdomain
93455 ! complexed with substrate peptide, chain B
93451 ! complexed with substrate peptide, chains B,C, D and E
53354 ! topological variant; strand order 3214567; strand 6 is antiparallel to the rest
108478 !SQ Q972K9
75265 ! function unknown
71846 ! structural genomics
64117 ! contains additional N-terminal beta-sandwich domain
62090 ! structural genomics
92482 ! structural genomics
102575 ! Pfam 01189; contains additional N-terminal 3-helical and ferredoxin-like domains
105913 !SQ P36929
105911 !SQ P36929
102578 ! contains additional N-terminal ferredoxin-like domain
99340 ! structural genomics
102581 ! Pfam 05958
102582 ! includes an iron-sulfur cluster-binding, alpha+beta sudbomain
53357 ! contains additional N-terminal all-alpha domain, res. 11-91
105675 !SQ P05102
106053 !SQ P05102
53375 ! an enigmatic DNA methyltransferase homologue from mitochondria
95511 ! complexed with DNA
53377 ! circularly permuted version of the common fold
69557 ! contains additional N-terminal tetramerisation all-beta domain, res. 1-71
69558 ! polyamine aminopropyltransferase 
76946 ! CASP5
79199 ! structural genomics
85587 ! structural genomics
108723 !SQ Q9KAF6 # ! Structural genomics target
108837 !SQ Q9X119 # ! Structural genomics target
102587 ! 3 layers, a/b/a; mixed beta-sheet of 7 strands, order 3214576; strand 7 is antiparallel to the rest; topological similarity to SAM-dependent methyltransferases
102589 ! putative deacetylases
102591 ! gene Rv1170
99136 ! structural genomics
53382 ! main domain: 3 layers: a/b/a, mixed beta-sheet of 7 strands, order 3245671; strand 7 is antiparallel to the rest
34275 ! CA-atoms only
89754 ! TM1255
86621 ! structural genomics
102594 ! TM1040
108041 !SQ Q9X0D0
106055 !SQ O15839
82482 ! cysteine sulphoxide lyase
108281 !SQ Q75WK2 
108285 !SQ Q75WK2 
108283 !SQ Q75WK2 
107544 !SQ P77806
109226 !SQ Q16773
109227 !SQ Q16773
109228 !SQ Q16773
104153 !SQ P13254
104144 !SQ O15565
53410 ! PLP-dependent haemolytic enzyme
53414 ! gene product CsdB
102598 ! alr1004
100827 ! structural genomics
106355 !SQ Q55793 # slr0077
53417 ! formerly omega-Aminoacid:pyruvate aminotransferase-like
105485 !SQ P22256
105469 !SQ P22256
105102 !SQ P07511
105107 !SQ P07511
105104 !SQ P07511
105109 !SQ P07511
82488 ! 4-amino-4-deoxy-L-arabinose liposaccharide modifying enzyme
53438 ! synonym: 7,8-diaminopelargonic acid synthase
92561 ! structural genomics
92537 ! structural genomics
92539 ! structural genomics
53447 ! 3 layers: a/b/a; mixed beta-sheet of 7 strands, order 3214657; strand 6 is antiparallel to the rest
105978 !SQ Q93EK7
108976 !SQ P14769
108974 !SQ P14769
75276 ! involved in blood group antigen biosynthesis
75278 ! involved in blood group antigen biosynthesis
108420 !SQ Q9P2W7
108416 !SQ Q9P2W7
108418 !SQ Q9P2W7
100605 ! structural genomics
100607 ! structural genomics
100617 ! structural genomics
100625 ! structural genomics
64144 ! capsule-specific enzyme
100635 ! structural genomics
100757 ! structural genomics
100639 ! structural genomics
53456 ! a sialic acid activating synthetase
107476 !SQ P26396
69571 ! 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 32145678; strands 6 and 8 are antiparallel to the rest
69572 ! transfer adenylyl group to the C-terminal carboxyl group of the ubiquitin and MoaD/ThiS-related proteins ! the ATP nucleotide-binding site is similar to that of the NAD-binding Rossmann-folds
89763 ! the common fold is elaborated with additional (sub)domains
89764 ! a subunit of the heterodimeric E1 enzyme for NEDD8; contains an all-alpha insert subdomain of the FF-like fold (residues 210-288) and an extra C-terminal alpha+beta subdomain (partly disordered)
107294 !SQ Q8TBC4 33-458
89766 ! a subunit of the heterodimeric E1 enzyme for NEDD8; contains a large insertion (residues 170-487) that can be divided into 3 units similar to the UBA3 insertion
107293 !SQ Q13564
53473 ! core: 3 layers, a/b/a; mixed beta-sheet of 8 strands, order 12435678, strand 2 is antiparallel to the rest
53474 ! many members have left-handed crossover connection between strand 8 and additional strand 9
63182 ! truncated recombinant enzyme
53488 ! bacterial homologue of human hormone sensitive lipase
108465 !SQ P31953
105502 !SQ P17944 43-330
99349 ! structural genomics
53496 ! N-terminal domain is a 7-bladed beta-propeller
108948 !SQ P23687
108946 !SQ P23687
82497 ! N-terminal domain is a 8-bladed beta-propeller
107072 !SQ P27487
104877 !SQ P27487
107113 !SQ P27487
90784 !SQ P27487 
107736 !SQ P27487
109050 !SQ P27487
53503 ! prohormone-processing carboxypeptidase
53504 ! synonyms: cathepsin A, carboxypeptidase L
82500 ! a novel cyanogenic enzyme
109405 !SQ O32449
77773 ! structural genomics ! CASP5
108859 !SQ Q9WXT2 # ! Structural genomics target
53522 ! closely related to the Proline iminopeptidase-like family
82507 ! 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase
107907 !SQ P96965 3-273
107909 !SQ P96965 3-273
107906 !SQ P96965 3-273
107910 !SQ P96965 3-273
107908 !SQ P96965 3-273
107905 !SQ P96965 3-273
89772 ! involved in carbazole degradation
78514 ! CASP5
107225 !SQ Q06174
102627 ! haloperoxidase homologue
110695 ! haloperoxidase homologue
108463 !SQ P22862
34734 ! CA-atoms only
34737 ! CA-atoms only
34762 ! CA-atoms only
102631 ! Triacylglycerol lipase homologue
107912 !SQ Q6ED33
53570 ! lack the first two strands of the common fold
64145 ! minimal alpha/beta hydrolase fold;
34778 ! open conformation
34779 ! open conformation
82512 ! the first thermostable bacterial lipase
53578 ! contains additional, colipase-binding domain
53583 ! pancreatic lipase related protein 1
53584 ! pancreatic lipase related protein 2
105421 !SQ P52704
105419 !SQ P52704
105420 !SQ P52704
105422 !SQ P52704
69585 ! syn.: 6-deoxyerythronolide synthase
52260 ! minimal alpha/beta hydrolase lacking peripheral secondary structures; similar to a flavodoxin-like fold
110699 ! lack the first two strands of the common fold  
108121 !SQ P96671 # RL 1ISP|P37957 (B-E); ! "stripped" alpha/beta hydrolase fold; 
108663 !SQ Q04066 # ! Structural genomics target
53589 ! core: 3 layers, a/b/a ; mixed beta-sheet of 8 strands, order 32145687; strand 7 is antiparallel to the rest
53596 ! 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 34251687; strand 8 is antiparallel to the rest
34894 ! CASP2
105463 !SQ list: Q5CGA3 Q27552 # 100% Identity
53612 ! core: 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest ! potential superfamily: members of this fold have similar functions but different ATP-binding sites
53613 ! has extra strand located between strands 2 and 3
88394 ! structural genomics
73222 ! structural genomics
82515 ! includes a variety of carbohydrate and pyrimidine kinases
100753 ! structural genomics
106766 !SQ P77150
108885 !SQ Q9X055 # ! Structural genomics target
71588 ! structural genomics
100250 ! structural genomics
100248 ! structural genomics
100254 ! structural genomics
100261 ! structural genomics
100850 ! structural genomics
80764 ! CASP5
107623 !SQ O59355 # PH1645
53623 ! has extra strand located between strands 1 and 2
82521 ! TM0231
77096 ! structural genomics
102644 ! TM0166
92531 ! structural genomics
102645 ! combination of the Rossmann-like and Ribokinase-like topologies; mixed beta-sheet of 8 strands, order 32145678, strand 7 is antiparallel to the rest 
64152 ! 3 layers: a/b/a; mixed (mainly parallel) beta-sheet of 8 strands, order 32145678; strand 8 is antiparallel to the rest
64153 ! possible circular permutation of the ribokinase-like fold (of the YjeF C-terminal domain)
63320 ! structural genomics
53632 ! 3 layers: a/b/a; mixed (mainly parallel) beta-sheet of 8 strands, order 34215786; strand 8 is antiparallel to the rest
53633 ! the sheet topology is similar to those of undecaprenyl diphosphate synthase and the N-terminal domain of phosphoglycerate kinase
34968 ! carbamate kinase-like carbamoyl phosphate synthetase
64157 ! core:3 layers: a/b/a; mixed beta-sheet of 8 strands, order 45321678, strands 4 and 5 are antiparallel to the rest
53648 ! core:3 layers: a/b/a; mixed beta-sheet of 8 strands, order 43516728, strand 7 is antiparallel to the rest
53650 ! common fold is decorated with several large insertions
105561 !SQ Q9BHT8 # fragment
105559 !SQ Q9BHT8 # fragment
53653 ! includes additional C-terminal alpha+beta (sub)domain
91559 ! covalent reaction intermediate
91560 ! covalent reaction intermediate
102649 ! contains membrane-anchoring alpha-hairpin insertion
102650 ! placental estrone/DHEA sulfatase
102651 ! contains alpha+beta subdomain inserted near C-terminus 
110709 ! 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 78612354; strands 3, 4 and 8 are antiparallel to the rest
110711 ! pfam04260, DUF436
110712 ! UPF0340 protein TTHA0583
108427 !SQ P68591 # ! Structural genomics target
69592 ! 3 layers: a/b/a; mixed beta-sheet of 9 strands, order 918736452; strands 1, 2 and 8 are antiparallel to the rest
69593 ! some topological similarity to the dihydropholate reductase fold
53638 ! 3 layers: a/b/a; mixed (mostly antiparallel) beta-sheet of 9 strands, order 432159876; left-handed crossover between strands 4 and 5
53640 ! metal (zinc)-ion dependent
53641 ! class II aldolase
95189 ! structural genomics
64166 ! 3 layers: a/b/a; mixed beta-sheet of 9 strands, order 342156798; strands 3, 8 and 9 are antiparallel to the rest; left-handed crossover connection between strands 6 and 7
64167 ! some topological similarity to the N-terminal domain of Glutaminase/Asparaginase family
64169 ! has a phosphatase activity
62763 ! complexed with vanadate
62761 ! complexed with tungstate
66207 ! structural genomics; target TM107
53658 ! consists of two intertwined (sub)domains related by pseudo dyad; duplication ! 3 layers: a/b/a; single mixed beta-sheet of 10 strands, order 213A945867 (A=10); strands from 5 to 9 are antiparallel to the rest
53659 ! the constituent families form similar dimers
53660 ! the active site is between the two identical subunits
108743 !SQ Q9WZ26 # ! Structural genomics target
106219 !SQ O75874
106198 !SQ O75874
102656 ! Pfam 04166; contains extra beta-alpha unit between strands 2 and 3; closer relationships to the PlsX-like and phosphotransacetylase families
102657 ! pyridoxal phosphate biosynthetic protein
102660 ! Pfam 02504; contains extra beta-alpha unit between strands 2 and 3; closer relationships to the PdxA-like and phosphotransacetylase families
100725 ! structural genomics
107727 !SQ Q82ZE8 # ! Structural genomics target
102663 ! Pfam 01515; contains extra beta-alpha unit between strands 2 and 3; closer relationships to the PdxA-like and PlsX-like families
97098 ! structural genomics
104673 !SQ P38503
82526 ! the active site is contained within one subunit between the canonical ICDH fold and a large insert domain that itself is a probable rudiment form of ICDH fold resulted from duplication, domain swapping and deletion
82528 ! the insert region spans residues 150-404
75303 ! possible duplication: the topologies of N- and C-terminal halves are similar; 3 layers: a/b/a; single mixed beta-sheet of 10 strands, order 213549A867 (A=10); strands from 5 to 9 are antiparallel to the rest
82531 ! elaborated fold with additional helices
53670 ! consists of two similar domains related by pseudo dyad; duplication ! core: 3 layers, a/b/a, parallel beta-sheet of 4 strands, order 2134
107342 !SQ P00479
104712 !SQ P00479
104576 !SQ P00479
107313 !SQ P00479
107300 !SQ P00479
104694 !SQ P00479
35201 ! CA-atoms only
104147 !SQ Q55338
108867 !SQ P96108 # ! Structural genomics target
53682 ! C-terminal extension is added to the N-terminal domain
53685 ! consists of two similar domains related by pseudo dyad; duplication ! core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 3214
75312 ! TM0665
92494 ! structural genomics
35297 ! CASP2
104067 !SQ P20132
105072 !SQ Q00740
64174 ! PLP-dependent hemoprotein
53696 ! 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 21345
69599 ! dimer of mono-domain subunits
66611 ! structural genomics
78574 ! structural genomics ! CASP5
100776 ! structural genomics
86123 ! structural genomics
100761 ! structural genomics
107085 !SQ Q9PNE6 # ! Structural genomics target
109523 !SQ Q9KPY2 # ! Structural genomics target
53698 ! duplication: consists of two SIS domains related by pseudo dyad
71591 ! structural genomics
107471 !SQ Q8ZWV0
107473 !SQ Q8ZWV0
53701 ! permutation of the double-SIS domain fold
53702 ! moonlights as neuroleukin, autocrine motility factor, and differentiation mediator
60397 ! complexed with 5-phosphoarabinonate, a transition state analogue
106235 !SQ P42861
104535 !SQ P42861
53705 ! contains of two similar intertwined domains related by pseudo dyad; duplication ! core: 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32451
53706 ! molybdopterine enzyme
53707 ! domain 1 (residues 1-55) binds Fe4S4 cluster in FDH but not DMSO reductase
35315 ! Tungsten-substituted
53718 ! dissimilatory nitrate reductase (NAP) 
105590 !SQ P09152
108813 !SQ P80563
106995 !SQ P80563
108789 !SQ P80563
106971 !SQ P80563
108765 !SQ P80563
106947 !SQ P80563
53719 ! consists of two similar domains with 3 layers (a/b/a) each; duplication ! core: parallel beta-sheet of 5 strands, order 32145
53720 ! binds NAD differently from other NAD(P)-dependent oxidoreductases
103933 !SQ P05091
89780 ! cytosolic form; eta-crystallin
108125 !SQ O57693
108120 !SQ O57693
108124 !SQ O57693
108126 !SQ O57693
108123 !SQ O57693
108127 !SQ O57693
108122 !SQ O57693
89782 ! TM0293
86556 ! structural genomics
108865 !SQ P54885 # ! Structural genomics target
53731 ! consists of three similar domains with 3 layers (a/b/a) each; duplication ! core: parallel beta-sheet of 5 strands, order 32145
53733 ! duplication: consists of three structurally similar subdomains with subdomains 1 and 3 being related by pseudo twofold symmetry
53737 ! consists of three similar domains with 3 layers (a/b/a) each; duplication ! core: mixed beta-sheet of 4 strands, order 2134, strand 4 is antiparallel to the rest
53742 ! consists of two domains of similar topology, 3 layers (a/b/a) each ! Domain 1 (1-173) has parallel beta-sheet of 5 strands, order 21345 ! Domain 2 (174-355) has parallel beta-sheet of 4 strands, order 2134
35449 ! CASP2
53747 ! consists of two non-similar domains, 3 layers (a/b/a) each ! Domain 1 has parallel beta-sheet of 6 strands, order 342156 ! Domain 2 has parallel beta-sheet of 6 strands, order 321456
53749 ! Domain 2 binds ATP
60058 ! Artificial circular permutation
53755 ! consists of two non-similar domains with 3 layers (a/b/a) each ! domain 1: parallel beta-sheet of 7 strands, order 3214567 ! domain 2: parallel beta-sheet of 6 strands, order 321456
63081 ! CA-atoms only
106100 !SQ P04547
106098 !SQ P04547
53761 ! UDP-N-acetylglucosamine:N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
100611 ! structural genomics 
92566 ! structural genomics 
64178 ! Glycosyltransferase family 28
105084 !SQ Q9AFC7 
88287 ! structural genomics
82540 ! family 20 glycosyltransferase; good structural similarity in the active site to the Oligosaccharide phosphorylases
53767 ! both domains are elaborated with many insertions
104066 !SQ P00489
104065 !SQ P00489
104064 !SQ P00489
108182 !SQ P00489 
105141 !SQ P39670
105143 !SQ P39670
53773 ! consists of two non-similar alpha/beta domains, 3 layers (a/b/a) each ! Domain 1 has mixed beta-sheet of 6 strands, order 213456, strand 6 is antiparallel to the rest; left-handed crossover connection between strands 4 and 5 ! Domain 2 has parallel beta-sheet of 4 strands, order 1234
53783 ! consists of two non-similar domains, 3 layers (a/b/a) each ! Domain 1 has mixed sheet of 7 strands, order 3214567; strands 3 & 7 are antiparallel to the rest ! Domain 2 has parallel sheet of 4 strands, order 2314
53786 ! Domain 1 binds ATP
53789 ! consists of two non-similar domains ! Domain 1 has parallel sheet of 5 strands, order 32415 ! Domain 2 has mixed sheet of 5 strands, order 12534; strands 4 & 5 are antiparallel to the rest
102684 ! diphthamide biosynthesis methyltransferase
82543 ! consists of two non-similar domains ! Domain 1 has parallel sheet of 6 strands, order 321456, Rossmann-like topology ! Domain 2 has mixed sheet of 6 strands, order 126345; strands 5 and 6 are antiparallel to the rest; some similarity to CbiF Domain 2
80744 ! CASP5
82548 ! 2 different domains; d1: [core: 3 layers, a/b/a; parallel sheet of 5 strands, order: 2134]; D2: [2 layers, a/b; mixed sheet of 6 strands, order 321645; strands 2 and 6 are antiparallel to the rest]
82549 ! domain folds and architecture show some similarity to the tubulin-like GTPases; the nucleotide-binding sites of the Dihydroxyacetone kinase and tubulin families are different 
82550 ! Pfam 02645, DUF194
82551 ! reveals fatty acid binding function
79098 ! structural genomics
102686 ! lipid-binding protein; Bacilus subtilis YitS ortholog
95485 ! structural genomics
109615 ! gene product YcgT
107971 !SQ P76015 20-366
107973 !SQ P76015 20-366
109616 ! contains additional alpha-helical, ATP-binding domain
64181 ! consists of two non-similar domains ! Domain 1 has parallel sheet of 6 strands, order 321456 ! Domain 2 has mixed sheet of 5 strands, order 12345; strands 1 & 4 are antiparallel to the rest
64182 ! constituent families have similar domain organization with variable interdomain linker and spatial arrangement of the domains
61868 ! CASP4
110737 ! consists of two different alpha/beta domains; (1) of the Flavodoxin-like fold (scop_cf 52171); (2) similar to the Restriction endonuclease-like fold (scop_cf 52979), inserted into domain 1
107171 !SQ P57098 # ! Structural genomics target
53794 ! contains a P-loop NTP-binding motif; mixed beta-sheet folds into a barrel-like structure with helices packed on one side
109391 !SQ Q7SIC6
72656 ! C-terminal domain in complex with P-Ser-HPr
72650 ! C-terminal domain in complex with HPr
62832 ! C-terminal domain only
68922 ! contains mixed beta-sheets; topology is partly similar to that of the catalytic C-terminal domain
109392 !SQ Q7SIC6
53799 ! duplication: tandem repeat of two domains; 3 layers (a/b/a); parallel beta-sheet of 4 strands, order 2134
53800 ! interdomain linker is short; swapping of C-terminal helices between the two domains
35594 ! CASP2
35596 ! CASP3
110742 ! single-domain protein; forms the C-terminal helix-swapped dimer similar to the CbiK subunit
107048 !SQ O29537 # ! Structural genomics target; AF0721
53807 ! contains a long alpha helical insertion in the interdomain linker
35597 ! complexed with gallichrome
72014 ! complexed with desferal
70132 ! complexed with coprogen
72105 ! complexed with albomycin-delta 2
71974 ! zn(ii)-free form
53816 ! contains three domains of this fold; "Helical backbone" holds domains 2 and 3 ! both chains are homologous; the inter-chain arrangement of domains 1 is similar to the intra-chain arrangement of domains 2 and 3
73590 ! FeMo-cofactor deficient
78451 ! chemically crosslinked structure
81401 ! both chains are homologous; the inter-chain arrangement of domains 1 is similar to the intra-chain arrangement of domains 2 and 3
73591 ! FeMo-cofactor deficient
78452 ! chemically crosslinked structure
69617 ! duplication: consists of two similar 'swapped' domain with 3 layers (a/b/a) each; parallel beta-sheet of 5 strands, order 21345
53821 ! consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication ! parallel beta-sheet of 6 strands, order 213456
53822 ! Similar in architecture to the superfamily II but partly differs in topology
106300 !SQ P18910 29-454
62907 ! complexed with a C-type natriuretic peptide, chain H
107062 !SQ Q8Z2X8 27-340
107149 !SQ Q8Z2X8 27-340
53849 ! consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication ! mixed beta-sheet of 5 strands, order 21354; strand 5 is antiparallel to the rest
53850 ! Similar in architecture to the superfamily I but partly differs in topology
53852 ! contains an additional alpha+beta domain inserted in the N-terminal domain
104103 !SQ P15712
53862 ! contains a few additional helices in the C-terminal extension; homologous to thiaminase I
106059 !SQ P02928
61240 ! fusion protein with SarR
106214 !SQ P02928
79113 ! chimera with yeast a1 homeodomain
80667 ! chimera with yeast L30e ribosomal protein
79115 ! chimera with yeast a1 homeodomain
35786 ! insertion/deletion mutant with an inserted B-cell epitope from hepatitis B virus
97174 ! chimera with a PAZ domain
35790 ! chimera with HTLV-1 gp21 ectodomain
35789 ! insertion/deletion mutant with an inserted B-cell epitope from hepatitis B virus
64191 ! trehalose maltose-binding protein
53865 ! contains a few additional helices in the C-terminal extension; homologous to MBP
105567 !SQ Q9Z4N6
105568 !SQ Q9Z4N6
109551 !SQ Q50964 23-331
53870 ! similar domain organization to oligopeptide-binding protein, OPPA
102692 ! similar domain organization to oligo- and dipeptide-binding protein
102694 ! similar domain organization to oligo- and dipeptide-binding protein
35806 ! CA-atoms only
82559 ! there is an additional C-terminal allosteric domain in some species
92541 ! structural genomics
92543 ! structural genomics
94384 ! structural genomics
97262 ! CASP5
108033 !SQ Q7WT50 75-301
108031 !SQ Q7WT50 75-301
110750 ! functionally related to the bacterial ProX
106072 !SQ O29280 # AF0982
106063 !SQ O29280 # AF0982
106068 !SQ O29280 # AF0982
106064 !SQ O29280 # AF0982
53888 ! further duplication: composed of two two-domain lobes
76674 ! N-terminal lobe
35836 ! N-terminal lobe
76673 ! N-terminal lobe
35842 ! N-terminal lobe
76672 ! N-terminal lobe
73602 ! N-terminal lobe
35858 ! N2-fragment (one domain fragment)
91943 ! C-terminal lobe
98812 ! C-terminal lobe
65606 ! domain II in the N-terminal lobe
65607 ! domain II in the N-terminal lobe
35875 ! domain II in the N-terminal lobe
62328 ! N-terminal lobe only
35880 ! N-terminal lobe only
35881 ! N-terminal lobe only
66261 ! C-terminal lobe only
35884 ! N-terminal lobe only
105129 !SQ P02789
35887 ! N-terminal lobe
98108 ! N-terminal lobe
35888 ! N-terminal lobe
59988 ! N-terminal lobe
35889 ! N-terminal lobe
35890 ! N-terminal lobe
67086 ! N-terminal lobe
35891 ! N-terminal lobe
87304 ! N-terminal lobe
85379 ! N-terminal lobe
85389 ! N-terminal lobe
59989 ! N-terminal lobe
85378 ! N-terminal lobe
35895 ! N-terminal lobe
87305 ! N-terminal lobe
35896 ! N-terminal lobe
35897 ! N-terminal lobe
35899 ! N-terminal lobe
53900 ! consists of two similar domains related by pseudo dyad; duplication ! 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32451; strand 5 is antiparallel to the rest
53903 ! topology of each domain is similar to the first domain of phosphoglucomutase
104032 !SQ P07097
103912 !SQ P14926
103920 !SQ P14926
84077 ! structural genomics
107258 !SQ Q02059
107260 !SQ Q02062
109261 !SQ P28790
109285 !SQ P28790
109273 !SQ P28790
106810 !SQ Q79FQ0 
106814 !SQ Q79FQ0 
110760 ! most similar to FabH
107368 !SQ Q7A3F6
107438 !SQ Q7A3F6
107560 !SQ Q9FCA7
102704 ! consist of two intertwined domains; duplication: contains two structural repeats of alpha-beta-(beta-alpha)3 motif with mixed beta-sheet, order: 1432, strand 1 is antiparallel to the rest
102705 ! di-iron binding protein
102706 ! Pfam 01784
91985 ! structural genomics
91991 ! structural genomics
53919 ! consist of two intertwined domains; contains partial duplication
53922 ! includes C-terminal region homologous to the smaller subunit of Desulfovidrio hydrogenase
89795 ! consist of two different alpha/beta domains; N-terminal domain has a SurE-like topology with a left-handed beta-alpha-beta unit
89797 ! forms interlocked homodimer of two ring-like subunits
108624 !SQ O06644
108626 !SQ O06644
106389 !SQ O06644
106411 !SQ O06644
96035 ! structural genomics
95094 ! structural genomics
95041 ! structural genomics
95090 ! structural genomics
96012 ! structural genomics
95096 ! structural genomics
53926 ! core: alpha-beta(2)-(alpha-beta)2; 3 layers (a/b/a); mixed beta-sheet of 4 strands, order 2134; strand 2 is antiparallel to the rest
108084 !SQ P19079
108082 !SQ P19079
108088 !SQ P19079
104815 !SQ Q06549 
53929 ! duplication: consists of two similar domains; contains extra helices in the N-terminal domain
109394 !SQ O34598
107013 !SQ O34598 ! Structural genomics target
102713 ! synonym Mov34, PAD-1; Pfam01398 
97133 ! structural genomics 
64197 ! duplication: consists of two domains of this fold with extra secondary structures within and in between the two core motifs
106924 !SQ P31335
53932 ! single helix packs against antiparallel beta-sheet
36222 ! trimeric domain swapped form
104392 !SQ Q53752
104388 !SQ Q53752
81310 ! the fungal cytotoxic ribonucleases with many insertions in the common fold
97056 ! delta(7-22) mutant
53954 ! common alpha+beta motif for the active site region
53961 ! ubiquitous in a variety of tissues and secretions
60688 ! Covalent glycosyl-enzyme intermediate
36299 ! CA-atoms only
36297 ! CA-atoms only
83298 ! complex with the E. coli Ivy
36315 ! neutron diffraction structure
85540 ! complexed with HYHEL-63
85545 ! complexed with HYHEL-63
36376 ! neutron difraction structure
36379 ! fused with a fragment of human fibrinogen gamma
105880 !SQ P00698
106597 !SQ P00698
109588 !SQ P00698
36397 ! CA-atoms only
36552 ! amyloidogenic variant
36566 ! amyloidogenic variant
108982 !SQ P00695
36586 ! apo-form
59452 ! holo-form
66033 ! holo-form
71442 ! lysozyme M
69627 ! induced antibacterial protein
53975 ! expressed only in the lactating mammary gland, strongly binds calcium ion
53983 ! many mutant structures
36890 ! an adaptable engineered metal-binding site
36936 ! contains an engineered tandem repeat
36955 ! contains an engineered tandem repeat
36807 ! Methionine core mutant
106663 !SQ P00720 ! engineered ligand-triggered molecular switch by sequence duplication
106709 !SQ P00720 ! engineered ligand-triggered molecular switch by sequence duplication
59112 ! complexed with a chitohexasacharide
53991 ! the large N-terminal domain is all-alpha superhelix
54000 ! consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn
54001 ! the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta-sheet
37024 ! zymogen with propeptide ! CASP2
54017 ! DNA-binding protease that has more insertions in the papain-like fold
37063 ! zymogen
81637 ! also contains a disulfide-bound minicathepsin H chain
107319 !SQ P43235 115-329
105819 !SQ P43235 116-329
37082 ! contains propeptide
37083 ! contains propeptide
37065 ! contains propeptide
37066 ! contains propeptide
37086 ! contains propeptide
95302 ! complexed with staphostatin B 
37093 ! zymogen
104328 !SQ P00788 31-398
54041 ! includes the N-terminal 'sequence' domain I
84935 ! calcium-bound protease core
73176 ! calcium-bound protease core
96550 ! mu-like isoform with the large and small subunits fused in a single chain
54046 ! Coagulation factor XIII
75333 ! GDP-binding protein
54047 ! fold similar to that of the factor XIII catalytic domain
80391 ! complex with ubiquitin aldehyde
108632 !SQ P43593 103-499
91962 ! complexed with peptide cofactor, chain B 
37132 ! complexed with peptide cofactor, chain B 
106904 !SQ Q9HC62 366-589
106901 !SQ Q9HC62 366-589
75336 ! inverted positions of the catalytic triad Asp and His residues
110773 ! probably the same as Pfam 02338, OTU-like cysteine protease, but 1TFF (SQ Q96DC9) was not detected by the Pfam model 
106854 !SQ Q96DC9
54059 ! core: (alpha)-beta-omega_loop-beta-alpha; embeded in larger different structures
54060 ! common motif contains conserved histidine residue and metal-binding site
93556 ! complexed with DNA
99476 ! computationally designed interface with the Im7 immunity protein
95088 ! complexed with DNA
108231 !SQ P09883 456-581
108239 !SQ P09883 456-581
108235 !SQ P09883 456-581
54066 ! the core motif is inserted in a six-stranded meander beta-sheet domain
37144 ! CASP1
107640 !SQ P34081
108204 !SQ O54788 85-329 # structure of the N-terminal, CAD domain (1-87) is solved separately; scop_sp 54282
54075 ! contains long curved beta-sheet and 3 helices
54076 ! can be classified as disulfide-rich
37164 ! deamidated derivative
37193 ! a new type of 3d domain swapping
37212 ! ASN 67 replaced by a beta-aspartyl residue
37230 ! semisynthetic
65740 ! domain-swapped dimer
37249 ! 3d domain-swapped dimer
71833 ! domain-swapped minor trimer
37254 ! chemical Ala 4 to Aib 'mutation'
37260 ! synthetic S peptide
37261 ! desiccated for 2.5 days
37262 ! desiccated for 4.0 days
37265 ! synthetic S peptide
37276 ! designed cytotoxic mutant
103975 !SQ Q9DFY5
103970 !SQ Q9DFY5
107211 !SQ P00669 27-150
96944 ! dimeric non-swapped form
70595 ! angiogenin/RNase A chimera ARH-I
99648 ! angiogenin/RNase A chimera ARH-II
54097 ! beta-alpha-beta-alpha(2); antiparallel beta-ribbon
66025 ! swapped dimer
107212 !SQ P23907 127-228
107189 !SQ P23907 127-228
107217 !SQ P23907 127-228
54105 ! beta-alpha(2)-beta; antiparallel strands
64209 ! alpha-beta(2)-alpha; antiparallel hairpin
110782 ! alpha-beta(2)-alpha; 2 layers a/b; antiparallel beta-hairpin 
104307 !SQ O26773 # ! Structural genomics target
54110 ! alpha(3)-beta(2); antiparallel hairpin
37335 ! CASP1
69631 ! fused with beta subunit
54116 ! beta(3)-alpha
54117 ! form dimers with different dimerisation modes
37369 ! monomeric mutant
37384 ! PF4-M2 chimeric mutant
37388 ! PF4-M2 chimeric mutant
54126 ! IL-8: residues 1-53; MGSA: residues 54-72
54128 ! has different dimerisation mode
66590 ! monomeric variant
54131 ! anti-HIV chemokine
54132 ! has different dimerisation mode
37411 ! synthetic, total chemical synthesis
54148 ! synonym: Small inducible cytokine B7; Neutrophil-activating peptide-2 (NAP-2), Connective tissue activating peptide-III (CTAP-III) 
54170 ! beta(3)-alpha; 2 layers: alpha/beta
62362 ! complex with methylated DNA
54183 ! alpha1-beta3; 2 layers: alpha/beta; order 132
54184 ! duplication: consists of 2 subdomains of this fold
37492 ! CA-atoms only
88797 ! beta-alpha-beta(2); 2 layers: alpha/beta; antiparallel beta-sheet: order 132
89808 ! Subunit assembly and a probable biological unit is a dodecamer, hence the name
54188 ! beta-(alpha)-beta-alpha-beta(2); 3 layers: alpha/beta/alpha; antiparallel beta-sheet: order 1243
105338 !SQ P12732
54193 ! elaborated with additional structures
105332 !SQ P60618
100965 ! beta-(2)-alpha(2)-beta(2); 2 layers: beta/alpha; antiparallel beta-sheet: order 1243; topological similarity to the common core of ribosomal proteins L23 and L15e
109089 !SQ P22257
106240 !SQ Q9KQS5
102740 ! beta-(2)-alpha(3)-beta(2); 2 layers: beta/alpha; mixed beta-sheet: order 1234; strands 2 and 3 a parallel to each other
102744 ! TT1381
54196 ! alpha-beta(3)-alpha-beta(2); 3 layers: alpha/beta/alpha
54198 ! topologically similar to the N-terminal domain of protein kinases
54207 ! duplication: consists of 2 HIT-like motifs ! binds zinc and iron ions
108694 !SQ Q9FK51 # ! Structural genomics target
108862 !SQ Q9DAR7 # ! Structural genomics target
69634 ! alpha-beta(3)-alpha-beta(2)-alpha; 2 layers: alpha/beta
69636 ! the family sequences are very divergent
68104 ! swapped oligomer
107308 !SQ Q7ARG9 #  ! complexed with YscM2 peptide (SQ O54481 37-56), chain B
105226 !SQ Q9K2L2 1-125
69649 ! duplication: tandem repeat of two domains of this fold
64495 ! beta(2)-alpha(2)-beta; 2 layers; 3-stranded antiparallel beta-sheet, order 213; HTH motif; also includes the extra N-terminal, DNA minor groove-binding helix
64498 ! contains extra N-terminal zinc-finger domain
106288 !SQ P13299 149-244
107641 !SQ P34081
69651 ! alpha-beta(4)-alpha-beta(2)-alpha; 2 layers: alpha/beta
89816 ! beta(4)-alpha-beta(2)-alpha; 2 layers: alpha/beta; antiparallel beta-sheet, order: 651234
54210 ! core: beta(3)-alpha-beta-alpha; 2 layers: alpha/beta; left-handed crossover
107619 !SQ P32324
82577 ! contains an H2TH domain inserted in front of this domain and after the N-terminal ATPase domain
102755 ! related to the DNA gyrase/MutL family; contains extra C-terminal alpha/beta subdomain
99885 ! complexed with Aha1
99893 ! complexed with Aha1
54230 ! duplication of two-domain units formed by domains 1-2 and 4-5
37579 ! CASP4
100769 ! structural genomics
89824 ! diverged from the GHMP Kinase family; lost the ATP-binding site
89827 ! duplication; there are two structural repeats of this fold; each repeat is elaborated with additional structures forming the active site
102766 ! duplication; there are two structural repeats of this fold
102769 ! contains extra C-terminal alpha/beta subdomain
102772 ! modification of the common fold; contains extra alpha-beta unit after strand 2, the extra strand is inserted between strands 3 and 4
102774 ! two-domain structure is similar to the C-terminal region of EF-G (domains IV and V)
100740 ! structural genomics
54235 ! core: beta(2)-alpha-beta(2); mixed beta-sheet 2143
54239 ! identical sequence in many other species
87001 ! synthetic protein with fluoro-Leu at 50 and 67
100239 ! annotated as bovine in PDB, identical to human sequence
37587 ! di-ubiquitin
80390 ! complex with USP7
37589 ! tetra-ubiquitin
37591 ! a new crystal form of tetraubiquitin
60319 ! Structure in aot reverse micelles
87751 ! annotated as bovine in PDB, identical to human sequence
105574 ! a multiple hydrophobic core mutant !SQ P62988
37593 ! designed hydrophobic core mutant
37594 ! designed hydrophobic core mutant
37596 ! nearly completely disordered chain D in the crystal structure
106902 !SQ Q93068
97010 ! complexed with APPBP1 and UBA3
97022 ! complexed with APPBP1 and UBA3
94388 ! complexed with the C-terminal ubiquitin-interacting motif of the proteasome subunit s5a
93442 ! flexible linkers excluded
99265 ! complexed with the C-terminal ubiquitin-interacting motif of the proteasome subunit s5a
104059 !SQ P54727 1-82
100275 ! structural genomics
108381 !SQ Q9DAF3 1-89 # ! Structural genomics target
108385 !SQ Q8BGR9 3-79 # ! Structural genomics target
108421 !SQ Q78JW9 76-157 # ! Structural genomics target
98459 ! complexed with the p97/VCP ND1; chain I is mostly disordered in the crystal structure
54253 ! intracellular membrane trafficking and fusion proteins
107827 !SQ Q62625 4-116
105531 !SQ P26038 4-297
83960 ! complexed with the icam-2 cytoplasmic peptide, chain B
69660 ! the neurofibromatosis 2 tumor suppressor protein
54274 ! includes parts of the flanking linkers
72180 ! complex with Ras
75362 ! Pfam 03671; this family contains a number of small uncharacterized proteins including human protein BM-002
73676 ! structural genomics
90740 ! structural genomics
54277 ! contain extra helix; similar heterodimerization modes; possibly related to the ubiquitin-like superfamily
62232 ! chimera with B1 domain of streptococcal protein G (disordered)
64225 ! Pfam 00564 ! forms heterodimers, although not all PB1 domain pairs associate.
88277 ! cloning artifact: lacks the N-terminal strand of the common fold and has a rearranged beta-sheet
108517 !SQ P41743 16-99
54285 ! possible link between the ubiquitin-like and 2Fe-2S ferredoxin-like superfamilies
37642 ! complexed with MoaE
37643 ! complexed with MoaE
67378 ! complexed with MoeB
86241 ! complexed with MoaE
67382 ! complexed with MoeB
67380 ! complexed with MoeB
108631 !SQ Q8U3C7 # ! Structural genomics target
107457 !SQ O31617
69664 ! probable ThiS homologue
98104 ! structural genomics
97991 ! structural genomics; low-resolution NMR structure
98826 ! structural genomics; low-resolution NMR structure
81271 ! possibly related to the ubiquitin-like and MoaD/ThiS superfamilies; some similarity to the alpha-L RNA-binding motif
82584 ! N-terminal domain belongs to the Obg family of GTPases some members of which contain a C-terminal TGS domain
89836 ! HI0393
84141 ! structural genomics
37676 ! CASP1
108740 !SQ Q46509
105582 !SQ Q46509
108443 !SQ P80457
54323 ! two other domains are common to ferredoxin reductase
72896 ! CASP4
106374 !SQ P72223
54331 ! phage-borne; Bacteriophage 42D
54332 ! duplication: consists of three similar domains
37724 ! domain B
77684 ! domain A
37728 ! domain B
77704 ! domain A
89837 ! possibly related to the ubiquitin-like superfamily
89839 ! KIAA0369; duplication: contains tandem repeat of two DC domains
84953 ! N-terminal DC domain
84940 ! N-terminal DC domain
99287 ! structural genomics; N-terminal DC domain
89841 ! duplication: contains tandem repeat of two DC domains
84977 ! N-terminal DC domain
59141 ! mutant vaccine
105653 !SQ P23313
105645 !SQ P23313
106494 !SQ P23313
108057 !SQ P08095
108267 !SQ Q9ZFS5 36-231
108271 !SQ Q9ZFS5 36-231
107445 !SQ Q7BAE3
107451 !SQ Q7BAE3
79134 ! redesigned protein variant nuG1
79136 ! redesigned protein variant nuG2
70131 ! Helix variant of the b1 domain
79512 ! X-ray structure of the intertwined tetramer resulted from a core mutation
79386 ! NMR structure of the intertwined tetramer resulted from a core mutation
59769 ! computationally designed core variant Delta0
37833 ! hyperthermophilic variant of the b1 domain
59768 ! computationally designed core variant Delta1.5
95527 ! segment-swapped dimeric mutant
68149 ! b1 domain
61431 ! b1 domain
61428 ! b1 domain
68147 ! b1 domain; mutation-induced segment swapping
68146 ! b1 domain; mutation-induced segment swapping
68605 ! b1 domain; computer-designed conformation in the second turn
79128 ! domain C
68151 ! b1 domain
60991 ! domain X; res. 820-880
37835 ! b1 domain
66887 ! b1 domain; an obligate dimer designed mutant
110814 ! possibly related to the ubiquitin-like and/or 2Fe-2S ferredoxin-like superfamilies
106222 !SQ O87799
106228 !SQ O87799
106225 !SQ O87799
54372 ! alpha+beta sandwich
54373 ! N-terminal domain is beta/beta/alpha common fold
79672 ! atomic resolution structure
54382 ! structurally very similar to PHBH, but contains additional C-terminal domain of the thioredoxin-like fold
106778 !SQ Q90W54 21-504
106776 !SQ Q90W54 21-504
106780 !SQ Q90W54 21-504
54399 ! Similar to FAD-linked reductases in both domains but does not bind FAD
107917 !SQ P39958 5-446
108597 !SQ P37727
108620 !SQ P37727
54402 ! Core: alpha-beta(4); helix packs against coiled antiparallel beta-sheet
54403 ! has a additional strand at the N-terminus
37989 ! single-chain version
80337 ! all-D monellin
90708 ! single-chain version
90710 ! single-chain version
68854 ! racemic DL-monellin structure
37996 ! single-chain version
84902 ! single-chain version
37997 ! single-chain version
60033 ! single-chain version
80342 ! segment-swapped dimer
104800 !SQ P01034 37-146 ! dimeric form with segment-swapping
60393 ! dimeric form with 3d domain swapping; only one monomer in the PDB entry
105024 !SQ P28325 31-142
105019 !SQ P28325 31-142
82592 ! cathelin-like domain
82593 ! antimicrobial protein
78291 ! swapped dimer
54417 ! duplication: contains two domains of this fold
105580 !SQ P46881 9-628
105577 !SQ P46881 9-628
84260 ! complexed with DsbD-alpha
106342 !SQ P45111 20-228
108374 !SQ P77202
108370 !SQ P77202
54427 ! has a beta-alpha(2)-beta insertion after the main helix
70747 ! complexed with FxFG nucleoporin repeat
89847 ! similar to the TAP domain; forms complex with MTR2 similar to the TAP-p15 complex
89848 ! Ypl169C
89849 ! similar to p15; forms complex with MEX67 similar to the TAP-p15 complex
89850 ! Ykl186C
98528 ! structural genomics
108980 !SQ P07445
108978 !SQ P07445
108981 !SQ P07445
107929 !SQ Q53123 11-187
107938 !SQ Q53123 11-187
82595 ! some sequence similarity to KSI
107345 !SQ Q99IU3
107184 !SQ Q9I430 # ! Structural genomics target
54441 ! has an additional strand at the C-terminus and a helix inserted after the first strand
102816 ! elaborated with additional structures; some similarity to Uracil-DNA glycosylase (UGI) and Nuclease A (NuiA) inhibitors 
102817 ! Pfam 04269, DUF440
102818 ! putative dsDNA mimic
92012 ! structural genomics
88802 ! this domain is found in association with the PUA domain in the C-terminal region of Archaeosine tRNA-guanine transglycosylase and related stand-alone proteins
88804 ! the second of the 3 additional C-terminal domains to the TGT-like domain, also includes "linker" C1 domain
102821 ! this protein is related to the C-terminal part (domains C2 and C3) of Archaeosine tRNA-guanine transglycosylase
96043 ! structural genomics
106496 !SQ Q9Y221 # RL 1Q7H|Q9HIB8 (B-E); 1J2B|O58843 (361-582)
82601 ! alpha-beta-alpha-beta-alpha(2)-beta(3); antiparallel beta-sheet; order: 15432
82602 ! some structural similarity to Uracil-DNA glycosylase inhibitor and putative dsDNA mimic HI1450 of the cystatin-like fold
102823 ! alpha(2)-beta(4)-alpha, 2 layers: alpha/beta, antiparallel beta sheet, meander
102826 ! tRNA-specific ribonuclease
110835 ! beta(3)-alpha-beta(2)-alpha; 2 layers, alpha/beta; antiparallel beta-sheet, order: 12543
104296 !SQ Q99U58
82606 ! core: alpha-beta(3)-alpha, 2 layers:alpha/beta, three-stranded antiparallel beta sheet, strand order 123
82607 ! forms tight dimer of a 3-layer structure: beta/alpha/beta
82608 ! Pfam 02575; DUF149; function unknown
88291 ! structural genomics
77101 ! structural genomics ! CASP4
102828 ! core: beta(2)-alpha(2), 2 layers: alpha/beta; long C-terminal helix forms dimeric parallel and tetrameric antiparallel coiled coils
102830 ! ZapA is a Z-ring associated protein first discovered in B. subtilis (formerly hypothetical protein YshA); Pfam 05164
99123 ! structural genomics
109124 !SQ Q9HTW3
54446 ! helix-swapped dimer of beta(4)-alpha motifs
54448 ! dimer of two separate motifs
75375 ! single-chain domain formed by a tandem repeat of two motifs
64233 ! beta-BETA(2)-beta-alpha-beta(2); antiparallel sheet: order 2134 packed against helix and BETA-hairpin on the same side; irregular C-terminal tail
54451 ! dimeric
105649 !SQ P01903 28-207
105641 !SQ P01903 28-207
106490 !SQ P01903 28-207
106486 !SQ P01903 28-207
76459 ! complexed with a peptide from epstein barr virus dna polymerase, chains C and H
78117 ! complexed with a peptide from hemagglutinin
98765 ! complexed with deamidated gliadin peptide
100063 ! complexed with a hypocretin peptide
63146 ! complexed with a human insulin peptide
79489 ! complex with a human clip peptide, chain C
76461 ! complexed with a peptide from Epstein barr virus DNA polymerase, chains C and H
78119 ! complexed with a peptide from hemagglutinin
105651 !SQ P04229 30-219
105643 !SQ P04229 30-219
106492 !SQ P04229 30-219
106488 !SQ P04229 30-219
98767 ! complexed with deamidated gliadin peptide
100065 ! complexed with a hypocretin peptide
63148 ! complexed with a human insulin peptide
59911 ! contains covalently bound peptides at the N-termini of chains B and D
59903 ! contains covalently bound peptides at the N-termini of chains B and D
38208 ! contains covalently bound peptides at the N-termini of chains B and D
61635 ! contains covalently bound peptides at the N-termini of chains B, D, F and H
72971 ! contains covalently bound peptides at the N-termini of chains B and D
72958 ! contains covalently bound peptides at the N-termini of chains B and D
38212 ! contains covalently bound peptides at the N-termini of chains B and D
79491 ! complex with a human clip peptide, chain C
74112 ! contains covalently bound peptides at the N-termini of chains B, D, F and H
38223 ! CA-atoms only
105392 !SQ P01892 25-298
105398 !SQ P01892 25-298
105395 !SQ P01892 25-298
104600 !SQ P13746 25-299 # 1A11_HUMAN HLA class I histocompatibility antigen, A-11 alpha chain precursor
104563 !SQ P13746 25-299 # 1A11_HUMAN HLA class I histocompatibility antigen, A-11 alpha chain precursor
54454 ! class I MHC-related
54456 ! Class I MHC-related
54487 ! fat depleting factor related to class I MHC
54489 ! gamma, delta T-cell ligand
75381 ! phospholipid-binding protein
74207 ! complexed with a phospholipid molecule and GLA domain of protein C
73690 ! complexed with a phospholipid molecule
104298 !SQ Q69G19 27-263 # 95% sequence identity
54494 ! alpha-beta(4)-alpha(3); core: meander beta-sheet plus one helix 2
107296 !SQ P21734
62818 ! complexed with Mms2
62819 ! complexed with ubc13
62681 ! complexed with Mms2
62680 ! complexed with ubc13
54503 ! identical sequence in many other species
38333 ! CASP2
102840 ! E2-17 kDa
102841 ! E2-17 kDa 2
78608 ! complex with a hiv-1 ptap "late domain" peptide
78607 ! complex with a hiv-1 ptap "late domain" peptide
107919 !SQ Q9QZ05 17-139 # ! Structural genomics target
63762 ! core: three short helices packed against a barrel-like beta-sheet; some similarity to the SH3-like fold
60642 ! CASP4
107817 !SQ Q8BVK9 353-433 # ! Structural genomics target
79421 ! complex with SMAD4 domain
110848 ! beta*-alpha-beta(2)-alpha-beta-alpha; mixed beta sheet forms a partly open barrel: (n*=4, S*=8)
108944 !SQ Q9LCY0 # Fragment
110853 ! contains insert domain (101-200) of an unusual alpha+beta fold beta-alpha-beta-alpha-beta(2)-alpha-beta-alpha-beta; 3 layers: a/b/a; antiparallel beta-sheet, order 516342; possibly related to Pfam 06245
108634 !SQ Q8U3S5
110856 ! beta-alpha-beta(4)-alpha-beta(2); contains beta-sheet barrel (n=5, S=8) 
108643 !SQ Q923B0 # ! Structural genomics target
102847 ! beta(3)-alpha(2)-beta; 2 layers; mixed beta-sheet, order 4123, strands 1 and 4 are parallel to each other
54505 ! mixed beta-sheet folds into a barrel (n=8, S=14) around the central helix
54506 ! duplication: consists of two similar domain swapped with C-terminal strands
89865 ! structural genomics; NESG target ET25
104652 !SQ P37757 # ! Structural genomics target
104656 !SQ P37757 # ! Structural genomics target
98808 ! structural genomics; NESG target ET25
98648 ! structural genomics
107550 !SQ Q9HV82 # ! Structural genomics target
110863 ! Pfam 05544
107148 !SQ Q8YFD6 # ! Structural genomics target
54510 ! beta-sheet folds into a barrel (n=11, S=14) around the central helix
93687 ! "gold" class of GFP; cyan fluorescent protein
93688 ! "gold" class of GFP; cyan fluorescent protein
73280 ! Zn biosensor, apo form
73288 ! Zn biosensor, Zn-bound form
73287 ! Zn biosensor, Cu-bound form
65685 ! a redox sensitive variant
77103 ! a dual-wavelength emission variant
93689 ! "gold" class of GFP; cyan fluorescent protein
61280 ! citrine, an improved yellow-emission variant
77102 ! a dual-wavelength emission variant
38345 ! blue-emission variant
105016 !SQ P42212
65795 ! Photoproduct of the wild-type GFP
79678 ! yellow-emission variant
105015 !SQ P42212
72843 ! cyclic variant with linked natural termini
38363 ! yellow-emission variant
38364 ! yellow-emission variant
105085 !SQ P42212
105012 !SQ P42212
105017 !SQ P42212
54517 ! beta-sheet folds into a barrel (n=12, S=12) around the central helix
61887 ! complexed to phosphatidylinositol 4,5-bis-phosphate
54522 ! contains very long N-terminal helix, which end is packed against beta-sheet
54523 ! bacterial filament proteins
104595 !SQ P17838 36-147
104923 !SQ P17838 36-147
104536 !SQ Q9ZIU9 51-206
89868 ! common fold is decorated with additional structures
87322 ! type IV pilin; classical biotype
54528 ! core: beta(7)-alpha(2); N- and C-terminal extensions form a coiled coil subdomain
82614 ! beta(6)-alpha; antiparallel beta-sheet, meander
82615 ! Serine/threonine protein kinase-associated motif embedded in two distinct folds
102856 ! duplication: consists of two polo-box domains; binds phosphothreonine peptide 
82616 ! beta(5)-alpha-beta; forms swapped dimer with two 6-stranded antiparallel beta sheets; order [6]123[4][5]
102859 ! beta(3)-alpha-beta(3)-alpha;  3 layers a/b/a
102860 ! forms swapped dimer with two 6-stranded antiparallel beta sheets; order 1236[5][4]
108863 !SQ Q9DAR7 # ! Structural genomics target
89871 ! alpha(2)-beta(5)-alpha(2); 3 layers a/b/a; meander beta-sheet
89874 ! formerly hypothetical protein YkfE
83296 ! complexed with lysozyme
100025 ! complexed with lysozyme
54533 ! core: beta(2)-alpha-beta(2); antiparallel beta-sheet
54536 ! cis-trans prolyl-isomerase
104475 !SQ Q02790 21-257 # ! tandem repeat of two FKPB domain
104073 !SQ Q02790 145-427 # ! second FKPB domain
104668 !SQ Q02790 145-427 # ! second FKPB domain
82621 ! duplication: tandem repeat of two FKBP domains
54547 ! Domain 1 is a WW-domain
85881 ! PPI domain only
89879 ! contains insert all-beta subdomain; dual function: PPI and chaperone-like activities
64250 ! contains all-alpha dimerisation subdomain in the N-terminal extension
102866 ! similar to MIP; contains all-alpha dimerisation subdomain in the N-terminal extension
109090 !SQ P22257
106241 !SQ Q9KQS5
107718 !SQ Q9SCY2 84-208
54550 ! N-terminal domain is a long alpha-hairpin
89882 ! secreted during involution
104042 !SQ P30922
104785 !SQ Q6TMG6
105947 !SQ Q6TMG6
106861 !SQ Q7YS85
54564 ! beta(4)-alpha-beta; 2 layers: alpha/beta; mixed beta-sheet, order: 51234
54569 ! alpha-beta-X-beta(2); 2 layers: alpha/beta; mixed beta-sheet, order: 123
54574 ! beta-alpha-beta-(alpha)-beta(2); 2 layers: alpha/beta; mixed beta-sheet, order: 1342
105343 !SQ P18138
54579 ! beta(2)-alpha-beta; 2 layers: alpha/beta
54584 ! beta-alpha-beta(3); 2 layers: alpha/beta
54587 ! NSF-N, the N-terminal 'functional' domain of the N-ethylmaleimide sensitive fusion protein, consists of two structural domains
54590 ! VAT-N is the N-terminal 'functional' domain of the VCP-like ATPase
93804 ! complete low resolution structure
109397 !SQ Q5BL07 13-179
54592 ! beta-alpha-beta(3); 2 layers: alpha/beta
54594 ! duplication: consists of two clear structural repeats each having this fold
54598 ! duplication: consists of two clear structural repeats each having this fold ! subunit fold and dimeric assembly are similar to those of glyoxalase
54599 ! Active as dimer
64256 ! the transposon tn5-encoding bleomycin-binding protein, BlmT
102871 ! gene from transposon tn2921
64257 ! Different association of repeats but a similar dimeric structure to the glyoxalase dimer
75396 ! Similar subunit fold is to methylmalonyl-CoA epimerase
72059 ! structural genomics
54602 ! duplication: consists of 2 similar domains with 2 repeats in each ! Similar to the Methylmalonyl-CoA epimerase dimer
38507 ! CASP1
88354 ! full length protein
106401 !SQ Q53586
106891 !SQ P93836 63-459
106887 !SQ P93836 63-459
105907 !SQ P93836 63-459
105876 !SQ P93836 33-428
105917 !SQ P32755
105875 !SQ O48604 29-423 # 85% sequence identity
110880 ! subunit fold and dimeric assembly are similar to those of glyoxalase 
105977 !SQ Q81F54
107725 !SQ Q9I3Y6 # ! Structural genomics target
107702 !SQ Q9I0C1 # ! Structural genomics target
110888 ! subunit fold and dimeric assembly are similar to those of glyoxalase 
107413 !SQ P37479
102874 ! beta(2)-alpha-beta(3); 2 layers: alpha/beta
74651 ! multiple repeats of beta(2)-alpha(2) motif
48403 ! repeats organized in elongated structures
79778 ! D34 region (12 repeats) and linker
69091 ! a member of the I-kappa-B family
48421 ! interrupted by an insertion
105317 !SQ Q90623 1-299
75399 ! repeats associate forming globular subdomains
74030 ! domain C (residues 2609-2822)
74032 ! domain B (residues 2209-2456)
89889 ! beta(2)-alpha(3)-beta; two layers: alpha/beta; antiparallel sheet: order 213
89892 ! processing of this protein releases peptide hormone guanylin, structure of which structure is known: see 1gna
54610 ! beta(4)-alpha(2); two layers: alpha/beta; antiparallel sheet: order 1432
89894 ! beta(2)-alpha(2)-beta(2)-alpha-beta; two layers: alpha/beta; antiparallel sheet: order 51234
86410 ! structural genomics; NESG target ytyst425
106706 !SQ O29759
104094 !SQ O29759 # ! Structural genomics target
75403 ! beta-alpha(2)-beta(4)-alpha-beta(2); two layers: alpha/beta; bifurcated coiled beta-sheet: order of the first 5 strands: 23154
54615 ! beta(4)-alpha(2)-beta(2)-alpha; antiparallel sheet: order 123465
54616 ! has some topological similarity to the "winged helix" DNA-binding domain, to B1 and B5 domains of PheRS-beta (1PYS CH B) and to methyl-CpG-binding domain
54620 ! beta-alpha-beta(6)-alpha(2); antiparallel sheet: order 165432
54625 ! beta(3)-alpha(2)-beta-alpha(2)-beta3; 2 layers alpha/beta; antiparallel sheet: order 1234567
102885 ! alpha-beta(6)-alpha(2)-beta-alpha(n); 3 layers alpha/beta/alpha; antiparallel sheet: order 1234567
102887 ! Pfam 01218
100836 ! structural genomics
107066 !SQ P11353
107106 !SQ P11353
107125 !SQ P11353
102890 ! beta(4)-alpha-beta(2)-alpha(2); mixed, predominately antiparallel beta-sheet, order: 123465, strands 4 and 5 are parallel to each other
102891 ! can be divided into an N-terminal, tetramerisation all-beta subdomain and a C-terminal alpha+beta subdomain related by a circular permutation to the Y-family DNA-polymerase 'fingers' subdomain
96456 ! structural genomics
54630 ! core: beta-alpha-beta(4); 2 layers: alpha/beta
54632 ! pairs of CBS domains dimerize to form a stable globular domain
92479 ! structural genomics
94415 ! structural genomics
102899 ! contains extra C-terminal zinc-finger domain
95175 ! structural genomics
54633 ! contains tandem repeat of two CBS domains inserted into the catalytic TIM-barrel domain; may be disordered in the crystals
84165 ! both CBS domains are partly disordered in both chains, A and B
91857 ! both CBS domains are partly disordered in both chains, A and B
91863 ! both CBS domains are partly disordered in both chains, A and B
54636 ! core: beta-alpha-beta(4); 2 layers: alpha/beta
85821 ! structural genomics
98580 ! structural genomics
92004 ! structural genomics
54641 ! contains two additional beta-strands in the N-terminal extension
38544 ! CASP1
54644 ! duplication: consists of two domains of this fold
82637 ! involved in polyhydroxyalkanoate (PHA) biosynthesis
96011 ! structural genomics
102907 ! duplication: consists of two MaoC-like domains; there is a greater structural divergence in the N-terminal domain
88286 ! structural genomics
98797 ! structural genomics; NESG target IR63
86533 ! structural genomics; NESG target IR63
100643 ! structural genomics
98794 ! structural genomics; NESG target ER29
100749 ! structural genomics
100654 ! structural genomics
90717 ! structural genomics
106642 !SQ Q8E989 # ! Structural genomics target
105550 !SQ Q9HUE3 # ! Structural genomics target
107607 !SQ Q9HXY7
54647 ! core: beta-alpha(2)-beta-X-beta(2); 2 layers: alpha/beta; antiparallel beta-sheet: order 1342
54649 ! 8 kDa dynein light chain, DLC8
54650 ! synonym: PIN, a protein inhibitor of neuronal nitric oxide synthase
38552 ! complex with a NOS peptide (residue 230-242)
38556 ! complex with a BIM peptide
38554 ! complex with a NOS peptide
54653 ! alpha+beta sandwich; loop across free side of beta-sheet
38561 ! cleaved between residues 45 and 46
38579 ! mutant with insertion (GQQQQGM) between met59 and glu60
69686 ! alpha-beta-loop-beta(3); loop across free side of beta-sheet
54664 ! core: beta-BETA-alpha-beta-BETA-beta-alpha; contains a beta-hammerhead motif similar to that in barrel-sandwich hybrids
108741 !SQ Q46509
105583 !SQ Q46509
108444 !SQ P80457
106375 !SQ P72224
89907 ! TM1645
86627 ! structural genomics
108846 !SQ P39683 # ! Structural genomics target
108847 !SQ P39683 # ! Structural genomics target
105327 !SQ P60617
38629 ! complexed with MoaD
38630 ! complexed with MoaD
86242 ! complexed with MoaD
54694 ! core: beta(2)-alpha(2)-beta(2)-alpha(2); 2 layers a/b; mixed sheet: 2143
61287 ! complexed with a von Hippel-Lindau peptide, chain B
82639 ! Suppressor of kinetochore protein 1,Scskp1
54712 ! beta(2)-alpha(n)-beta; 2 layers a/b; antiparallel sheet: 123
54716 ! duplication: consists of two subdomains of this fold
38680 ! dimer of a one subdomain fragment
54718 ! alpha-beta(2)-alpha-beta-alpha(2); 3 strands of antiparallel sheet: 213
38700 ! iron-substituted
54732 ! active with either fe or mn
107797 !SQ P19665
107805 !SQ P19665
54735 ! beta-alpha(2)-beta-alpha-beta; 2 layers, alpha/beta
78930 ! complex with ClpA N-domain
78924 ! complex with ClpA N-domain
79092 ! complex with ClpA N-domain
78312 ! complex with ClpA N-domain
78926 ! complex with ClpA N-domain
75411 ! beta-alpha-beta(2)-alpha(2); 3 layers, alpha/beta/alpha; antiparallel beta-sheet: order 123
71277 ! structural genomics
54746 ! beta-alpha(2)-beta(2); 2 layers, alpha/beta; antiparallel beta-sheet: order 123
54751 ! alpha-beta(3)-alpha(2); 2 layers, alpha/beta
107744 !SQ P03017 
107746 !SQ P03017 
107748 !SQ P03017 
38772 ! Hoess A., EMBO J. 12:3351, 1993
54761 ! (beta)-alpha-beta(3)-alpha; 2 layers, alpha/beta
38777 ! low resolution structure of potential alu retroposition intermediate
83028 ! single polypeptide chain construct with a SRP14 domain and linker, res. 3001-3008
38778 ! low resolution structure of potential alu retroposition intermediate
83029 ! single polypeptide chain construct with SRP9 and linker, res. 3001-3008
54767 ! alpha-beta(3)-alpha; 2 layers: alpha/beta
38781 ! complexed with dsRNA
38782 ! CASP1
54774 ! contains tandem repeat of two dsRBD
80754 ! CASP5
106426 !SQ Q02555 363-443
106423 !SQ Q02555 366-453
106424 !SQ Q02555 364-447
107855 !SQ Q9D5N7 3-78 # ! Structural genomics target
82645 ! contains N- and C-terminal extensions to the common fold involved in the oligomerization
82646 ! forms an undecameric ring structure; binds to ssDNA and dsDNA
54779 ! lacks the N-terminal helix
54788 ! contains additional C-terminal helix
110917 ! related to domain 3 of the Polypeptide chain release factors RF1 and RF2 (scop_fa 75621)
103823 !SQ Q8R035 63-162 
110920 ! duplication: consists of two beta(3)-alpha repeats; 3 layers, beta/alpha/beta 
105965 !SQ P96420
69694 ! beta-alpha-beta(2)-alpha; 2 layers: alpha/beta
79045 ! a part of a ternary s-domain complex
82648 ! alpha(2)-beta(3)-alpha(3); 2 layers alpha/beta, 3-stranded antiparallel beta-sheet; order 123
82649 ! iron-sulfur cluster assembly proteins
82650 ! Fe-S metabolism associated domain
82651 ! unknown function; probably involved in Fe-S center assembly
79697 ! structural genomics
85738 ! structural genomics; NESG target ER75
95783 ! structural genomics; NESG target IR24
106015 !SQ Q9A1G2 # ! Structural genomics target
89914 ! alpha(3)-beta-alpha(2)-beta(2); 2 layers alpha/beta, 3-stranded antiparallel beta-sheet; order 123
89918 ! MTH916
86092 ! structural genomics; NESG target TT212
54790 ! beta-alpha(2)-beta(2)-alpha; 2 layers: alpha/beta
54791 ! Prokaryotic and eukaryotic domains share a KH-motif but have different topologies
54792 ! an RNA-binding domain
110927 ! duplication: tandem repeat of two KH-1 domains
107322 !SQ Q9YE16
54805 ! core: alpha-beta(2)-(alpha)-beta; 2 layers: alpha/beta
54808 ! duplication: consists of two domains of this fold
54814 ! Prokaryotic and eukaryotic domains share a KH-motif but have different topologies
69701 ! duplication: tandem repeat of two type II KH-domains
54803 ! the type of KH-domain fold (II or I) adopted by this domain is not ascertained yet
38810 ! partly disordered
38811 ! partly disordered
82653 ! possible distant relative of the Era C-terminal domain lacking the KH motif
89919 ! possible distant homologue of the type I KH domain lacking the KH motif
84411 ! structural genomics
89923 ! HI1288
84191 ! structural genomics ! CASP4 ! RbfA homologue MPN156
94409 ! structural genomics
71169 ! structural genomics
82658 ! Pfam 01722
100542 ! structural genomics
103876 !SQ P43781 # ! Structural genomics target
81302 ! core: alpha-beta-turn-beta-X-beta-(alpha); mixed beta-sheet, order of core strands: 123
102932 ! insert X in the core is an alpha-helix; minimal nucleotidyltransferase fold 
102933 ! nucleotide binding subunit of the HI0073/HI0074 nucleotidyltransferase (see 1jog)
92015 ! structural genomics
102936 ! structural genomics
109470 !SQ P83814 # 100% identical to SQ Q72I47 (TTC1285)
56708 ! insert X in the core is a beta-strand ; mixed 4-stranded sheet, order: 1243
75881 ! CA-atoms only, mutant protein sequence
81589 ! insert X in the core is an alpha-beta(2) unit; mixed 5-stranded sheet, order: 12543
104549 !SQ P25500 18-497
104546 !SQ P25500 18-497
102937 ! similar overall structure to the first two domains of poly(A) polymerase, PAP 
102940 ! similar overall structure to poly(A) polymerase, PAP
106872 !SQ O28126
106884 !SQ O28126
106137 !SQ O28126
81300 ! insert X in the core is an alpha-beta(2) unit; mixed 5-stranded sheet, order: 12543; contains extra C-terminal alpha+beta subdomain
82661 ! overlaps with the N-terminal part of Pfam 01743; this family is distinct from eukaryotic PAPs ! insert X in the core is an alpha-beta(2) unit; contains two extra C-terminal strands; mixed 7-stranded sheet, order: 7612543
108573 !SQ O66728 443-824 # chain B coverage
102945 ! Pfam 04607; ppGpp-synthetase
110933 ! Pfam coverage excludes the extra N-terminal subdomain but includes a short segment of the next domain 2  
110934 ! includes extra N-terminal all-alpha subdomain (2-61) structurally similar to the PABP domain (scop_fa 63571)
108351 !SQ P30870 1-437 
54820 ! alpha(2)-beta(4); 2 layers: alpha/beta; antiparallel beta-sheet: order 2143
69704 ! alpha-beta(3)-alpha-beta-alpha; bifurcated coiled beta-sheet
54825 ! beta(3)-alpha(3); meander and up-and-down bundle
54827 ! C-terminal domain is beta/alpha-barrel
106800 !SQ P09104
107104 !SQ O34508
97929 ! structural genomics
105639 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
105631 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
105623 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
105615 !SQ Q44244 # similar activity to a remotely related O-succinylbenzoate synthase from E. coli
104754 !SQ Q9RYA6
54842 ! beta-alpha(3)-beta(2); 2 layers: alpha/beta; related to the enolase/MLE N-domain fold by a circular permutation
54843 ! some topological similarity to prokaryotic ribosomal protein L17
105337 !SQ P10970
64262 ! alpha-beta-alpha(3)-beta(2); 2 layers: alpha/beta;
64263 ! some topological similarity to ribosomal protein L22
54848 ! 3-helical bundle packed against 3-stranded mixed beta-sheet
109329 !SQ P61491
109381 !SQ P61491
64267 ! beta(3)-alpha(4); meander beta-sheet packed against array of helices; contains Pro-rich stretch
65681 ! complexed with phosphatidylinositol 3-phosphate
69720 ! beta(3)-alpha(5); meander beta-sheet packed against array of helices
54856 ! beta-alpha-beta(2)-alpha; 2 layers: alpha/beta; mixed sheet 213; crossing loops
110941 ! alpha-beta(3)-alpha(3); 2 layers, a/b; mixed beta-sheet, order:132; crossing loops
105479 !SQ P10413 511-624
54861 ! alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2
54863 ! contains two 4Fe-4S clusters
54870 ! has C-terminal extension to the common fold
38988 ! artificial Fe8S8 ferredoxin
38989 ! artificial Fe8S8 ferredoxin
54875 ! the N-terminal extension to the common fold forms a part of a Zn-binding site
54877 ! contains only one 4Fe-4S cluster
105596 !SQ P29603
105594 !SQ P29603
54884 ! members of this "family" may be more closely related to other ferredoxins than to each other
54891 ! includes linker from domain 4
69726 ! includes N-terminal partly folded tail
105591 !SQ P11349
108815 !SQ P80564
106997 !SQ P80564
108791 !SQ P80564
106973 !SQ P80564
108767 !SQ P80564
106949 !SQ P80564
107343 !SQ P00478
104713 !SQ P00478
104587 !SQ P00478
107314 !SQ P00478
107301 !SQ P00478
104705 !SQ P00478
104148 !SQ 
54902 ! procarboxypeptidase A2
54905 ! decorated with additional structure
39068 ! CASP1
106245 !SQ Q8RR56 
54909 ! dimerizes through the beta-sheet; forms beta-sheet barrel, closed (n=8, S=12); dimers may assemble in higher oligomers
95823 ! structural genomics
95859 ! structural genomics
107284 !SQ Q9AR79
105573 !SQ Q9AR79
102959 ! subfamily of Pfam 03992
90702 ! structural genomics
105909 !SQ Q99X56 # ! Structural genomics target
107465 !SQ Q81C15 # ! Structural genomics target
96201 ! structural genomics; monomeric form?
102965 ! structural similarity to MLI extends to the active site cavity location
91482 ! structural genomics
54910 ! decamer: pentamer of dimers
39070 ! CA-atoms only
69733 ! octamer: tetramer of dimers
102968 ! archaeal feast/famine regulatory protein
102969 ! identical sequence to Pyrococcus sp. ot3 protein
107346 !SQ P39890
110962 ! there is the putative active site cavity in the equivalent location location to the MLI and YciI active sites 
105353 !SQ Q9I3Z5 # ! Structural genomics target
110965 ! duplication: consists of two similar domains; forms a pentamer similar to the MLI decamer 
106233 !SQ Q5KUD5 # 98% sequence identity; Geobacillus kaustophilus TaxID:1462
108527 !SQ Q5SHL6 # ! Structural genomics target
110970 !  subfamily of Pfam 03992
109503 !SQ Q9HY51 # ! Structural genomics target
54913 ! form timeric structures with the orthogonally packed beta-sheets
54915 ! trimer with orthogonal packing of beta-sheets around the threefold axis
99343 ! structural genomics
86444 ! structural genomics
100382 ! structural genomics
87695 ! structural genomics
72889 ! structural genomics
100671 ! structural genomics
92503 ! structural genomics
92480 ! structural genomics
82669 ! binds allosteric inhibitor histidine
76863 ! structural genomics
39087 ! CASP1
54930 ! duplication: contains two domains of this fold
107598 !SQ P09651 7-188
107599 !SQ P09651 7-188
107597 !SQ P09651 7-188
107596 !SQ P09651 7-188
107595 !SQ P09651 7-188
107594 !SQ P09651 7-188
107593 !SQ P09651 7-188
107592 !SQ P09651 7-188
71279 ! domain 1
54932 ! duplication: contains two domains of this fold
80732 ! contains a pre-organized C-terminal helix
39155 ! domain 1
39157 ! domain 1
39158 ! domain 1, complex with a hepatitis delta virus ribozyme
39159 ! domain 1, complex with a hepatitis delta virus ribozyme
39164 ! domain 2
78655 ! domain 1, complex with a ribozyme
105601 !SQ P09012 1-98
78663 ! domain 1, complex with a ribozyme
74510 ! domain 1, complex with a hairpin ribozyme
108497 !SQ P09012 1-98
108492 !SQ P09012 1-98
78657 ! domain 1, complex with a ribozyme
105602 !SQ P09012 1-98
108489 !SQ P09012 1-98
108490 !SQ P09012 1-98
105646 !SQ P09012 1-98
108496 !SQ P09012 1-98
108491 !SQ P09012 1-98
108495 !SQ P09012 1-98
39163 ! domain 1 !SQ P09012 4-98
107703 !SQ P09012 1-97
93406 ! third RNA-binding domain; complexed with an N-terminal Sf1/Mbbp peptide, chain B
86535 ! third RNA-binding domain; complexed with an N-terminal Sf1/Mbbp peptide, chain B
39167 ! second RNA-binding domain
39168 ! first RNA-binding domain
39179 ! first RBD
39180 ! second RNA-binding domain
39181 ! the first RNA-binding domain (RBD1)
39182 ! the second RNA-binding domain (RBD2)
39187 ! RBD1
39188 ! RBD1
39189 ! RBD2
39190 ! RBD2
105661 !SQ P26599 54-141, 177-284 # coverage for 1SJQ and 1SJR, respectively; structure of the RR3-RR4 domains (335-531) is 1QM9
105660 !SQ P26599 54-141, 177-284 # coverage for 1SJQ and 1SJR, respectively; structure of the RR3-RR4 domains (335-531) is 1QM9
39208 ! representative structure
39212 ! RBD2
39209 ! RBD1
89939 ! CG8781 protein 
102978 ! RBM8A, Y14
98632 ! central RBD
87494 ! C-terminal RBD
93899 ! N-terminal RBD
99358 ! structural genomics
39213 ! disordered
39215 ! chain E domain disordered
63180 ! heterodimer with a fragment U2AF65 subunit; chain B
102987 ! Pfam 03467
54959 ! forms dimers with subunit beta-sheets making (8,12) barrel
54964 ! DNA-binding mode differs from that of E2 protein
54966 ! C-terminal domain is beta/alpha barrel
109128 !SQ P84142
107998 !SQ Q9VF36
54981 ! domain III structure is lacking some of the superfamily characters and is often disordered in crystals
54982 ! domain III is seen in 1FNM but disordered in the most of other PDB entries
107621 !SQ P32324
102991 ! similar to EF-G domain V; N-terminal domain shares structural similarity with the EF-G domain IV
100741 ! structural genomics
106707 !SQ O29759
104095 !SQ O29759 # ! Structural genomics target
89942 ! elaborated with additional structures
39322 ! mutant engineered for aggregation
39325 ! mutant engineered for aggregation
39326 ! mutant engineered for aggregation
82682 ! interrupted by an insert beta-sandwich domain
92363 ! N-terminal domain (Ngn) only
104550 !SQ P25500 18-497
104547 !SQ P25500 18-497
102995 ! decorated fold with a large insertion
106873 !SQ O28126
106885 !SQ O28126
106138 !SQ O28126
104023 !SQ list: O66016 Q58AI1 Q5NUU9 Q6UP70 Q7BRH5 Q7BRH6 Q7X3A5 # 100% identity
75441 ! duplication: contains tandem repeat of two HMA domains in the N-terminal region
72880 ! domain 2
93412 ! domain 1
93414 ! domain 1
93407 ! domain 1
71919 ! domain 2
60046 ! apo form
60049 ! Cu(I) form
39341 ! 4th metal-binding domain
96214 ! 2nd metal-binding domain
98608 ! 2nd metal-binding domain
91043 ! 1st metal-binding domain
91042 ! 1st metal-binding domain
98597 ! 2nd metal-binding domain
39342 ! 4th metal-binding domain
59800 ! apo form
59770 ! Cu(I) form
55021 ! regulatory domain linked to a wide range of metabolic enzymes
55026 ! duplication: consists of two homologous domains
39357 ! CASP2
95953 ! nickel-bound; C-terminal domain only
95944 ! apo form 
110980 ! tandem repeat of two ACT-like domains; swapped domain dimer
107740 !SQ Q9KQ45 # ! Structural genomics target
55033 ! dimerisation mode is similar to that of 1PSD domain
100780 ! structural genomics 
100623 ! structural genomics
82685 ! contains insert sudbomain 205-292 mimicking the other half of the family-specific dimer
106192 !SQ P13702 4-377 # chain B coverage
110983 ! structurally distinct from the E.coli domain and possesses a different CheY-binding mode 
107565 !SQ Q56310 175-260
72911 ! structural genomics
107899 !SQ Q72J47
107895 !SQ Q72J47
107897 !SQ Q72J47
86381 ! structural genomics
103010 ! structural genomics
82689 ! the last strand of the fold is flipped away and involved in oligomerisation
55060 ! common fold is elaborated with additional secondary structures
39401 ! CASP4
100770 ! structural genomics
89953 ! lost the ATP-binding site
89954 ! primary determinant of sexual fate in C. elegans
55064 ! common fold is elaborated with additional secondary structures
55068 ! common fold is elaborated with additional secondary structures
55073 ! common fold is elaborated with additional secondary structures
55074 ! structurally similar to the "palm" domain of DNA/RNA polymerase superfamily
39430 ! variant Gresag 4.1
39431 ! variant Gresag 4.3
55083 ! common fold is elaborated with additional secondary structures
39433 ! CASP3
69742 ! common fold is elaborated with additional secondary structures
89958 ! Pfam 01910; unknown function ! two domains form a single beta-sheet dimer; two dimers pack sheet-to-sheet in a tetramer; contains extra C-terminal helix
84740 ! structural genomics; NESG target TT272
84736 ! structural genomics; NESG target Ytyst72
108639 !SQ Q9WYV6 # ! Structural genomics target
110987 ! duplication: one subunit consists of two domains assembled as in the MHT1178-like dimer
105352 !SQ O34911 # ! Structural genomics target
55088 ! each of the three different subunits, alpha, beta and gamma, contains this fold decorated with additional secondary structures
55094 ! C-terminal domain is all-alpha
55103 ! duplication: contains two subdomains of this fold
109061 !SQ P56216
109065 !SQ P56216
109057 !SQ P56216
109069 !SQ P56216
55107 ! the other subunit is a short-chain cytochrome c
109071 !SQ Q9T0N8
109073 !SQ Q9T0N8
109075 !SQ Q9T0N8
109077 !SQ Q9T0N8
55112 ! duplication: contains two subdomains of this fold
55116 ! duplication: contains two subdomains of this fold
55124 ! duplication: contains two subdomains of this fold
82693 ! duplication: the N- and C-terminal halves of the whole proteins are structurally similar; each half contains two domains of this fold
82695 ! PN2 and PC2 subdomains are interrupted by the inserted subdomains DN and DC, respectively
89963 ! duplication: consists of two domains of this fold swapped with their N-terminal strands
83697 ! structural genomics ! CASP5
104557 !SQ P05198 
110997 ! duplication: one domain contains two repeats of similar sequence and structure 
108029 !SQ P29131 243-319
109622 ! consists of two alpha+beta subdomains with some similarity to the ferredoxin-like fold  
82697 ! segment-swapped dimer: the swapped segment is made of the first helix and second strand; a single long strand is formed by strands 2 and 3 of each subunit
82700 ! MTH169
76345 ! structural genomics
106405 !SQ P12049 
107410 !SQ P12049 # Hypothetical protein yexA
111002 ! duplication: consists of 2 structural repeats of the PurS subunit fold, assembled like the PurS dimer 
106383 !SQ P74881
111005 ! beta-alpha-beta-X-beta(2)-alpha(2)-beta; antiparallel beta-sheet, order 24153; topological similarity to the ferredoxin-like fold (scop_cf 54861)
107611 !SQ Q62165 58-303
100877 ! consists of two alpha+beta subdomains with some similarity to the ferredoxin-like fold  
55120 ! the active site is the most conserved structural region of the superfamily and is located between the subdomains
69746 ! contains C-terminal PUA domain
75459 ! contains N-terminal alpha-L RNA-binding motif
100764 ! structural genomics 
108448 !SQ P33643
108450 !SQ P23851
103021 ! natural circular permutation in the catalytic domain; insertion of the family-specific alpha+beta subdomain
103023 ! family-specific insert subdomain: res. 158-301
105409 !SQ Q57261
103024 ! duplication: consists of two beta(2)-alpha-beta(3)-alpha subdomains swapped with the first strands 
103025 ! some topological similarity to Formylmethanofuran:tetrahydromethanopterin formyltransferase
108872 !SQ P39179 # ! Structural genomics target
92090 ! structural genomics
109469 !SQ Q9WY54
109467 !SQ Q9WY54
109461 !SQ Q9WY54
109459 !SQ Q9WY54
108839 !SQ P27248 # ! Structural genomics target
103031 ! duplication: contains two similar beta-x-beta(4) motifs swapped with the first strands 
95150 ! structural genomics
100878 ! beta-alpha-beta(2)-alpha-beta; antiparallel beta-sheet: order 1423; "reversed" ferredoxin-like topology
99681 ! little finger domain only complexed with DNA polymerase III beta subunit
106365 !SQ Q9UNA4
106703 !SQ Q9UBT6 71-517
55128 ! core: beta-alpha-beta-alpha-beta; antiparallel beta-sheet: order 312; some similarity to the ferredoxin-like fold
55131 ! short-chain member of the family
55133 ! long-chain member of the family; contains additional C-terminal (sub)domain
105342 !SQ P14121
64287 ! duplication of alpha(2)-beta(3) motif; antiparallel beta sheet, order 123654
60059 ! tight complex with product; CASP4
55135 ! duplication of beta-alpha-beta(2) motif: antiparallel beta sheet forms barrel (n=6, S=12)
71956 ! structural genomics
104844 !SQ P39075
103038 ! duplication: tandem repeat of two intertwined alpha-beta-(BETA)-beta(2) motifs; dimer
103040 ! Pfam 04509
103042 ! TM1618
98972 ! structural genomics
55143 ! duplication of beta-alpha-beta-alpha-beta motif: antiparallel beta sheet forms barrel (n=6, S=8) similar to the barrel of prokaryotic DNA topoisomerases I and III
39538 ! CASP4
89969 ! TT0787
83711 ! structural genomics
55148 ! duplication of beta(3)-alpha(2) motif: meander beta sheets form barrel-like structure
55153 ! duplication of beta-alpha-beta(3) motif: antiparallel beta sheet forms wide barrel (n=8, S=16) with a channel running through it
55158 ! beta(2)-alpha-beta(2)-alpha-beta; 2 layers: alpha/beta; mixed beta-sheet: order 51243
55165 ! alpha-beta(2)-alpha-beta(2); 2 layers: alpha/beta
55166 ! zinc-binding motif
107521 !SQ P14007
107575 !SQ P14007
104792 !SQ Q06241
55173 ! alpha(2)-beta(2)-loop-beta; 2 layers: alpha/beta
55174 ! common motif in otherwise different folds
55178 ! has a RRF/tRNA synthetase additional domain-like fold
55179 ! also contains a Zn-binding N-terminal subdomain
55182 ! there are additional C-terminal structures
55183 ! ribosome-binding protein
75465 ! there are additional N-terminal structures
103046 ! overall topological similarity to the TyrRS C-domain
100765 ! structural genomics 
55185 ! core: alpha-beta(2)-alpha-beta(2); 2 layers: alpha/beta
55186 ! putative editing domain found in the N-terminal part of ThrRS, the C-terminal of AlaRS, and as a stand-alone protein; probable circular permutation of LuxS </i>(<a href="../search.cgi?sccs=d.185.1.2">d.185.1.2</a>)<i>
103052 ! stand-alone protein related to the AlaRS domain
63410 ! core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta
63411 ! Share the same "active site motif" HxxEH located in the first core helix, but differ in one of the zinc-binding residues
64294 ! contains additional N-terminal strand; possible relationships to the putative editing domain of ThrRS </i>(<a href="../search.cgi?sccs=d.67.1">d.67.1</a>)<i>
64295 ! S-ribosylhomocysteinase 
100808 ! structural genomics
100619 ! structural genomics
100636 ! structural genomics
63412 ! Common fold elaborated with many additional structures; duplication: each family member consists of two similar domains of beta(2)-alpha(2)-beta(2)-alpha(5)-beta structure, but only the N-terminal domain of MPP beta chain binds the catalytic metal
104268 !SQ P31800
104238 !SQ P31800
105891 !SQ P31800
104270 !SQ P23004
104240 !SQ P23004
105893 !SQ P23004
55199 ! beta-alpha-beta-alpha-beta(2); 2 layers; mixed sheet 1243, strand 4 is antiparallel to the rest
62057 ! complexed to 30S ribosomal subunit; CA-atoms only
75472 ! Pfam 1985
74043 ! structural genomics
77141 ! structural genomics
105056 !SQ Q99TQ4 # ! Structural genomics target
88852 ! predicted redox protein, regulator of disulfide bond formation
64309 ! implicated in cell division
64310 ! formerly hypothetical protein YhhP
59115 ! structural genomics
88013 ! structural genomics
71637 ! structural genomics
66559 ! structural genomics
82706 ! an archaeal chromatin protein modulated by acetylation, a Sir2 substrate
82707 ! gene SSO0962 (AlbA1)
103058 ! gene SSO6877 (AlbA2)
103059 ! gene AF1956
108874 !SQ O22969 19-117 # ! Structural genomics target
64586 ! contains a metal (zinc)-binding site
82708 ! possibly lacks the N-terminal strand of the common fold
82709 ! Pfam 01424 ! predicted nucleic acid-binding domain
107825 !SQ Q8VDG3 162-248 # ! Structural genomics target; structure of an RNA-binding domain (430-516) is also known: 1whv 
55206 ! duplication: 3 repeats of this fold are packed together around the pseudo threefold axis
55207 ! also contains an insert alpha+beta domain of the thioredoxin-like topology
39569 ! CASP3
55209 ! duplication: 6 repeats of this fold are organized in two RPTC-like domains
39586 ! CA-atoms only
69753 ! beta-alpha-beta(3)-alpha; 2 layers; mixed sheet 1234, strand 3 is antiparallel to the rest
69756 ! Ribosome associated factor; cold-shock response protein
69757 ! HI0257
66218 ! structural genomics
74652 ! beta(2)-alpha-beta; 2 layers, alpha/beta; left-handed beta-alpha-beta unit in non-swapped monomer
55217 ! contains extra N-terminal helix
39587 ! Fused with the N-terminal domain of gp3 from phage M13
64326 ! Segment-swapped dimer; forms single coiled antiparallel beta-sheet
55220 ! beta-alpha-beta(2)-alpha-beta(2); 2 layers, alpha/beta; left-handed crossover connection
55226 ! cleaved into alpha and beta chains
55228 ! dimer of alpha-beta(2) motifs ; 2 layers, alpha/beta
103062 ! dimer of beta(2)-alpha motifs ; 2 layers, alpha/beta; reverse MinE topology
103067 ! dimer of alpha-beta(2)-alpha motifs ; 2 layers, alpha/beta
55233 ! intertwined dimer of alpha-beta(2) motifs ; 2 layers, alpha/beta
55235 ! active form is a decamer formed by five dimers
39605 ! CASP3
82713 ! Intertwined pseudo hexamer of an alpha+beta motif
82714 ! duplication: the N- and C-terminal halves of the whole proteins are structurally similar
55238 ! alpha-beta(2)-alpha-beta(2); 2 layers, alpha/beta
55247 ! beta(2)-alpha-beta(2)-alpha; 2 layers, alpha/beta
55248 ! has additional alpha helix at the N-terminus
55252 ! forms trimers with three closely packed beta-sheets
55257 ! form homo and heterodimers
105786 !SQ Q9Z9H6 #! part of multichain biological unit
55262 ! has additional structures inserted in the common fold loops
100886 ! beta(2)-alpha-beta(2)-alpha; 2 layers, alpha/beta; mixed beta-sheet 2143, strands 1 and 4 are parallel
85369 ! structural genomics
55266 ! beta(2)-alpha-beta(2)-alpha-beta(2); 2 layers, alpha/beta
103073 ! duplication: one subunit consists of two tetrameric tRNA splicing endonuclease subunit-like repeats
39744 ! CASP4
109225 !SQ P23909 2-800
55276 ! beta(2)-alpha-beta(2)-alpha; 2 layers, alpha/beta
77662 ! complexed with proline-rich CD2 tail segment peptide, chain B
69760 ! beta(2)-alpha-beta(2)-alpha-beta(2); 2 layers, alpha/beta, antiparallel beta-sheet: order 342165
109491 !SQ P70552
55281 ! beta-alpha-beta(2)-alpha-beta(3)-alpha; 2 layers, alpha/beta; antiparallel beta-sheet: order 231654
55284 ! synonym: 50S ribosomal protein L5p, HMAL5, HL13
79209 ! complex with a 5S rRNA fragment
105322 !SQ P14124
55286 ! core: beta-alpha-beta-alpha-beta(2); 2 layers, alpha/beta
39752 ! probably incorrect structure
55297 ! core: beta-alpha-beta-alpha-beta(2); mixed beta-sheet: order: 1423, strand 4 is antiparallel to the rest
55298 ! forms trimers with three closely packed beta-sheets; possibly related to the IspF </i>(<a href="../search.cgi?sccs=d.79.5">d.79.5</a>)<i> and 4'-phosphopantetheinyl transferase superfamilies </i>(<a href="../search.cgi?sccs=d.150.1">d.150.1</a>)<i>
55299 ! some members possess an endoribonuclease activity inhibiting mRNA translation
39757 ! contains phosphorylated cysteine
82719 ! YjgF homologue HI0719
94604 ! structural genomics
89979 ! mammalian tumor associated antigen UK114
103078 ! Perchloric acid soluble protein
69765 ! forms trimers with three closely packed beta-sheets; possible link between the YjgF-like </i>(<a href="../search.cgi?sccs=d.79.1">d.79.1</a>)<i> and 4'-phosphopantetheinyl transferase superfamilies </i>(<a href="../search.cgi?sccs=d.150.1">d.150.1</a>)<i>
107643 !SQ P36663
107644 !SQ P36663
107647 !SQ P36663
107653 !SQ P36663
100652 ! structural genomics
100660 ! structural genomics
71756 ! structural genomics
86975 ! complexed with SulA homologue PA3008
105051 !SQ O08378
104987 !SQ O08378
105055 !SQ O08378
107363 !SQ P02550
107365 !SQ P02554
106215 !SQ P14120
80668 ! fusion protein with MBP
105325 !SQ P12743
105441 !SQ P54066
104982 !SQ O29494 # AF0764
75481 ! 23S rRNA methyltransferase; proposed gene names are as appear in the original publication (and the PDB entry)
82721 ! 23S rRNA G2251 2'O-methytransferase
55324 ! contains a large insertion forming a separate (sub)domain
103082 ! duplication: tandem repeats of two PurM-like units arranged like the PurM subunits in the dimer 
103083 ! TM1246
100847 ! structural genomics
106385 !SQ P74881
103089 ! Pfam 00691
111037 ! beta(2)-alpha-beta(2)-alpha(2)-beta(3); contains a beta-sandwich: 7 strands in 2 sheets; trimerizes with orthogonally packed beta-sheets
109540 !SQ Q97KL0 # ! Structural genomics target
55330 ! (beta-alpha-beta)2; 2 layers: alpha/beta; mixed beta-sheet ! generally forms trimers with three closely packed beta-sheets
55332 ! dimer of beta-alpha-beta subunits: may assemble further in hexamer (trimer of the dimers)
103094 ! forms heterohexamer with beta-subunit
103096 ! forms heterohexamer with alpha-subunit
82723 ! forms stable dimer without further oligomerisation
55340 ! synonym: glycosylation-inhibiting factor (GIF)
107887 !SQ Q76BK2
39864 ! CASP3
103098 ! lacks the N-terminal proline
91485 ! structural genomics
107750 !SQ Q9KU16
55346 ! core: alpha-beta-alpha-beta(3); mixed sheet: 2134, strand 2 is parallel to strand 1
55347 ! N-terminal domain is the classic Rossmann-fold
55348 ! has many additional secondary structures
105347 !SQ P06977
89987 ! formerly Alcaligenes xylosoxidans
39908 ! CASP3
105005 !SQ P19866
105011 !SQ P19866
104999 !SQ P19866
106409 !SQ P00353
106417 !SQ P00353
104046 !SQ P44801
104287 !SQ P44801
104309 !SQ P44801
104301 !SQ P44801
104506 !SQ P44801
104295 !SQ P44801
104305 !SQ P44801
108683 !SQ Q9X2A2 # ! Structural genomics target
107357 !SQ P31116
55366 ! contains an alpha-helical subdomain inserted in the common fold and other additional secondary structures
55369 ! distantly related to dihydrodipicolinate reductase ! larger alpha+beta subdomain substitutes for one helix and one strand of the common fold
108883 !SQ Q9X1K8 # ! Structural genomics target
104993 !SQ P11986
107589 !SQ O28480
108685 !SQ Q18664 # ! Structural genomics target
103105 ! myo-inositol 1-phosphate synthase-related protein
100829 ! structural genomics
104442 !SQ P45568
104469 !SQ P45568
106269 !SQ P45568
106277 !SQ P45568
104457 !SQ P45568
104734 !SQ Q9X5F2
104746 !SQ Q9X5F2
55376 ! has many additional secondary structures
55377 ! very similar to the glucose 6-phosphate dehydrogenase domain
107138 !SQ P75931 # ! Structural genomics target
109579 !SQ Q9KKQ4
111056 ! alpha-beta-alpha-beta(4); 2 layers: a/b; mixed beta-sheet, order 23145, strands 1 and 3 are parallel; similar to the GAPDH C-terminal domain-like fold (scop_cf 55346)
105551 !SQ Q8U2E0 # ! Structural genomics target
55382 ! alpha-beta(5)-alpha; 2 layers: alpha/beta; meander antiparallel sheet
55385 ! non-conserved N-terminal domain
55388 ! iron homeostasis proteins
55389 ! protein responsible for Friedreich ataxia
103108 ! Pfam 05303
98857 ! structural genomics; NESG target HR969
55393 ! core: [beta]-alpha-beta(5)-alpha; 2 layers: alpha/beta; antiparallel beta-sheet, meander
103111 ! consists of a single domain of this fold
99886 ! complexed with a Hsp90 domain
99894 ! complexed with a Hsp90 domain
55394 ! duplication: consists of two clear structural repeats of this fold also containing an extra C-terminal beta-hairpin
40027 ! CASP2
55398 ! alpha+beta sandwich
40030 ! CA-atoms only
55404 ! 6-standed beta-sheet followed with 2 helices; meander
40131 ! contains 9 more identical chains denoted "!, #, _, -, =, :, <, >, |"
55417 ! beta(2)-alpha-beta(2)-alpha-beta(2)-alpha-beta-2; 2 layers: alpha/beta; antiparallel sheet: 21356478
55420 ! messenger RNA 5' cap-binding protein
97370 ! complexed with eIF4g fragment
55423 ! core: beta(3,4)-alpha(3); alpha+beta sandwich
55424 ! both first two domains are of same beta/beta/alpha fold
75489 ! contains a large loop insertion in this domain
55443 ! rudiment "interface" domain of smaller size; beta(3)-alpha
108445 !SQ P80457
106377 !SQ P72222
55454 ! alpha-beta(2)-alpha; dimer; 3 layers a/b/a; antiparallel beta-sheet
91687 ! complexed with a cabin 1 peptide, chain G
55463 ! alpha-beta-alpha-beta(2)-alpha-beta-alpha-beta; 3 layers: a/b/a; antiparallel sheet 41325
103120 ! circular permutation of the common fold
111063 ! alpha(2)-beta-alpha(2)-beta(3); 3 layers: a/b/a; antiparallel beta-sheet: order 1234
111066 ! an RNA-binding antitermination protein
108530 !SQ P10943
111068 ! beta-alpha(2)-beta-alpha(2)-beta(2)-alpha(n)-beta; 3 layers: a/b/a; antiparallel beta-sheet, order: 21543
105125 !SQ P76483 # ! Structural genomics target
111073 ! alpa-beta(3)-alpha-beta(3)-alpha; 3 layers: b/a/b, 3-helical bundle flanked by two 3-stranded meander beta-sheets
104838 !SQ Q81EU2 # ! Structural genomics target; 100% sequence identity to a Bacteriophage phBC6A51 protein 
55468 ! core: (alpha-beta-alpha-beta)2; 3 layers a/b/a; antiparallel beta-sheet: 1243
111078 ! duplication: consists of two similar domains arranged as the subunits of the dimeric NADH oxidase/flavin reductase with one conserved active site
108695 !SQ Q9X1S2 # ! Structural genomics target
55480 ! alpha-beta-alpha(2)-beta(3)-alpha; 3 layers a/b/a; antiparallel beta-sheet: 4123
55485 ! contains mixed beta sheet with connection over free side of the sheet
55487 ! single domain
64335 ! single domain with insertions in the common fold
55490 ! includes alpha-helical C-terminal domain characteristic for the family
107670 !SQ P14756 198-495
104123 !SQ P00800
104125 !SQ P00800
104124 !SQ P00800
73537 ! an open conformation in the absence of substrate
64338 ! adopts thermolysin-like fold
105943 !SQ P09960 
55503 ! contains thermolysin-like catalytic domain (residues 419-749) ! the N-terminal half of the structure is multihelical
104756 !SQ P08473 54-749
104758 !SQ P08473 54-749
104757 !SQ P08473 54-749
55505 ! combines M2, M3 and M32 families of metalloproteases ! the N-terminal half of the structure is multihelical; the C-terminal half contains the thermolysin-like catalytic domain
55506 ! M3 family member; the thermolysin-like catalytic domain consists of residues 352-674
105252 !SQ P52888
82731 ! M32 (Taq) family member; overall fold is similar to that of neurolysin but is less elaborated
82733 ! M2 family member; overall fold is similar to that of neurolysin but is less elaborated
108174 !SQ P22966 
108175 !SQ P22966 
96968 ! complexed with collectrin homology domain (disordered segments), chains B, C, D and E
96998 ! complexed with collectrin homology domain (disordered segments), chains B, C, D and E
69776 ! duplication: each domain adopts a thermolysin-like fold, but the proteolytic activity resides only in the C-terminal domain
95248 ! complexed with small molecule inhibitor 
95236 ! complexed with small molecule inhibitor 
95260 ! complexed with an optimized peptide substrate (chains C and D) in the presence of zinc
95254 ! complexed with an optimized peptide substrate (chains C and D) in the presence of zinc
95242 ! complexed with small molecule inhibitor 
66818 ! complexed with the n-terminal peptide of mapkk2
55500 ! the catalytic domain is N-terminal (residues 100-272) ! the rest of structure will be classified in future releases
55508 ! characteristic HEXXHXXGXXH motif and Met located near C-terminus
55509 ! the rest of protein is all-beta sandwich containing a parallel beta-helix
55510 ! alkaline protease
55511 ! Serralysin
82735 ! Protease C
82736 ! psychrophilic alkaline protease
83168 ! catalytic domain only; cleaved
106344 !SQ Q00496 1-421
106340 !SQ Q00496 1-421
109435 !SQ P20165
59043 ! truncated proenzyme
103132 ! COG0319; MMP-like fold with a different sequence motif in the putative active site
93808 ! structural genomics 
55545 ! contains similar fold but lacks its catalytic centre
55546 ! family GH20
82737 ! family GH67
82738 ! inverting reaction mechanism
55549 ! 3 layers: a/b/a; antiparallel beta-sheet of 5 strands is flaked by two helices
55551 ! Pfam 00017
93893 !  complexed with peptide, chains C and D
86454 ! complexed with doubly phosphorylated peptide, chain C
86458 ! complexed with doubly phosphorylated peptide, chain C
77173 ! complex with the Crk-derived phophopeptide and Abl SH3 domain
40498 ! C-terminal SH2 domain
40500 ! C-terminal SH2 domain
40499 ! C-terminal SH2 domain
87184 ! N-terminal SH2 domain
40502 ! N-terminal SH2 domain
40501 ! N-terminal SH2 domain
87185 ! N-terminal SH2 domain; complexed to a peptide derived from PDGFR (chain B)
60837 ! complexed with a tyr751 phosphopeptide from the pdgf receptor
40519 ! C-terminal SH2 domain
40520 ! C-terminal SH2 domain
40537 ! complex with a slam peptide
40543 ! complex with slam phosphopeptide
84748 ! complex with Fyn SH3 domain and slam peptide, chain B
68371 ! complex with peptide
83667 ! complex with slam phosphopeptide, chain B
97763 ! complexed with insulin receptor kinase
104962 !SQ Q13882 75-174
104764 !SQ O89100 53-147
104762 !SQ O89100 53-147
104768 !SQ O89100 53-147
55593 ! beta-alpha-beta(2)-alpha-beta-alpha; 2 layers: a/b; antiparallel sheet 1423
72659 ! P-Ser protein complexed with HprK/P kinase domain
72653 ! complexed with HprK/P kinase domain
40551 ! contains phospho-serine 46
40564 ! CASP1
91366 ! N-terminal strand-swapped dimer 
91461 ! N-terminal strand-swapped dimer 
71593 ! structural genomics
90001 ! beta-alpha-beta(4)-alpha; 2 layers: a/b; antiparallel sheet 15234; topological similarity to the HPr-like fold
90004 ! homologue of the cobalamin biosynthesis protein CobW
85742 ! CASP5 ! structural genomics
69785 ! beta(2)-loop-alpha-beta(2)-alpha; 2 layers: a/b; antiparallel sheet 1243; some similarity to the Homing endonuclease-like fold
80326 ! structural genomics ! CASP5
67136 ! structural genomics
55603 ! alpha-beta(2)-alpha-beta(2)-alpha; 2 layers: a/b; antiparallel sheet 1243
55607 ! there are differences in secondary structure packing between the two NMR-determined structures
55609 ! contains two extra helices in the C-terminal extension
60409 ! DNA product complex with magnesium
60407 ! DNA substrate complex with calcium
79366 ! chimera with the I-dmoI N-domain
55612 ! duplication: contains tandem repeat of this fold
79367 ! chimera of N-domain with I-CreI
103141 ! duplication: contains tandem repeat of this fold
103142 ! synonym: Emericella nidulans
55614 ! duplication: contains tandem repeat of this fold
55615 ! homing endonuclease with protein splicing activity
107951 !SQ P17255 284-737
55619 ! beta(2)-alpha(2)-beta(2); 2 layers: alpha/beta; antiparallel sheet 1234 ! tunnel-shaped: its known members form wide oligomeric barrels different sizes
55620 ! bind purine or pterin in topologically similar sites between subunits
55622 ! beta-sheets of five subunits form a barrel, closed: n=20, S=20
40631 ! zinc-containing active form
109481 !SQ P22288
55626 ! beta-sheets of three subunits form a barrel, closed: n=12, S=12
55628 ! beta-sheets of four subunits form a barrel, closed: n=16, S=16
105940 !SQ Q9SF23
55634 ! duplication: one subunit consists of two domains of this fold; beta-sheets of two subunits form a barrel, closed: n=16, S=16
103828 !SQ Q45697 177-482
55636 ! beta(2)-alpha(2)-beta(2); 2 layers: alpha/beta; antiparallel sheet 1243 ! can form strand-exchange dimers
55640 ! in hexamer, the beta-sheets of three dimers form a barrel, closed: n=12, S=12
55647 ! alpha(2)-beta(4); 2 layers: alpha/beta
55649 ! duplication: consists of two clear structural repeats each having this fold
55652 ! alpha-beta-alpha(2)-beta(2); 2 layers: alpha/beta
55657 ! beta(2)-alpha-beta-alpha; 3 layers: alpha/beta/alpha
70073 ! N-domain only
103144 ! beta(2)-alpha-beta(2)-alpha; 2 layers: alpha/beta; antiparallel sheet: order 2134
103147 ! an RNA silencing suppressor
97257 ! complexed with siRNA
97717 ! complexed with siRNA
55665 ! beta(2)-alpha-beta(2)-alpha; 3 layers: alpha/beta/alpha; antiparallel sheet: order 2134
55668 ! duplication of two-domain units formed by domains 1-2 and 4-5
55670 ! alpha(2)-beta(4)-alpha; 3 layers: alpha/beta/alpha
55675 ! core: beta-alpha(2)-beta-alpha(2)-beta(4); 3 layers: a/b/a
104214 !SQ Q6USC4
104221 !SQ Q6USC4
55680 ! contains large mixed beta-sheet
55685 ! contains an insertion of LEM/SAP-like HeH motif, residues 337-379
90008 ! non-discriminating and archaeal-type enzyme
55703 ! this domain is non-catalytic
75505 ! TM0216
71590 ! structural genomics
103158 ! AspRS-related protein 
92005 ! structural genomics
55708 ! this structure contains an SH2-like fold
61365 ! complexed with biotin
55710 ! beta-alpha-beta-alpha-beta(4)-alpha; 3 layers: a/b/a; bifurcated antiparallel beta-sheet
40791 ! CASP3
55717 ! alpha-beta(3)-(crossover)-beta-(alpha)-beta; 3 layers: a/b/a; antiparallel beta-sheet of 5 strands; order: 32145
103164 ! core: beta-alpha-beta(2)-alpha-beta-alpha-beta; 3 layers: a/b/a; antiparallel beta-sheet of 5 strands; order: 51423; 
97646 ! structural genomics
55723 ! (beta-hairpin)-beta(3)-alpha-beta(4)-alpha; 3 layers: a/b/a; antiparallel beta-sheet of 7 strands; order: 1237654
108280 !SQ P18212
111095 ! segment-swapped dimer; some sequence similarity to the PsbP-like family
107317 !SQ Q9I738 # ! Structural genomics target
55728 ! 3 layers: a/b/a; contains mixed beta-sheet
82747 ! possesses HAT activity
78398 ! complex with bisubstrate analog inhibitor
40806 ! complex with coenzyme A and histone H3 peptide
104497 !SQ Q27198 49-209
95129 ! complex with coenzyme A and histone H3 peptide, chain B
95130 ! complex with coenzyme A and a phosphorylated histone H3 peptide, chain B
104496 !SQ Q27198 49-209
55742 ! contains additional N- and C-terminal (sub)domains
55744 ! most similar to HAT1 including the N- and C-terminal (sub)domains; the N-terminal domain contains a rudiment CCHC zinc-finger (res. 191-220); the C-terminal domain (res. 351-434) has "winged helix" DNA-binding fold
88486 ! structural genomics
87098 ! structural genomics; target SR144
84980 ! structural genomics
86142 ! structural genomics
95655 ! structural genomics; NYSGRC target T804
100699 ! structural genomics
97080 ! structural genomics; NESG target ZR31
103175 ! duplication: consists of two NAT domains swapped with the C-terminal strands with both domains binding acetyl-CoA; structural link with the other families
103176 ! Rv0819 
105251 !SQ Q9R381
105277 !SQ Q9R381
105282 !SQ Q9R381
107011 !SQ P21340 # ! Structural genomics target
55748 ! duplication: consists of two NAT-like domains swapped with the C-terminal strands
62427 ! complex with s-(2-oxo)pentadecyl-CoA and the octapeptide
105023 !SQ P33883
82749 ! duplication: consists of two NAT-like domains swapped with the C-terminal strands
82750 ! transfer glycyl residue from tRNA-Gly
103179 ! duplication: consists of two NAT-like domains swapped with the C-terminal strands
98966 ! structural genomics; NESG target FR87
55752 ! 3 layers: a/b/a; contains mixed beta-sheet
55759 ! consists of six similar domains
104930 !SQ Q28372 1-346
68449 ! metal ion-binding domain 2
40846 ! domain 1 ! domain 1
40851 ! domain 1
106395 !SQ P20065 55-179
80653 ! domain 1
80632 ! domain 1
80658 ! domain 1
94373 ! domains 4, 5 and 6
79017 ! domain 1
94376 ! domain 1 with a domain 2 linker
76505 ! domains 4, 5 and 6
85958 ! domains 4, 5 and 6 in active, actin free conformation
40848 ! domain 1
40850 ! domain 1
104558 !SQ P23528
104555 !SQ P23528
55768 ! identical sequence in both species
82752 ! interacts only with G-actin
107780 !SQ Q9CQI6
109436 !SQ Q14019 
108395 !SQ Q9CQI3
108669 !SQ Q9ERL7 # ! Structural genomics target
94510 ! complexed with a snare peptide
94500 ! complexed with a snare peptide
94505 ! complexed with a snare peptide
55769 ! core: 2 alpha-helices and 5-stranded antiparallel sheet: order 21543; 3 layers: alpha/beta/alpha
55770 ! alpha-beta(2)-alpha-beta(5)-alpha
55781 ! alpha(2)-beta(3)-alpha-beta(3)-alpha; antiparallel beta-sheet: order 321654
40896 ! structural genomics
82760 ! GAF B is the nucleotide binding domain; the two domains are connected with a long helix;
100692 ! structural genomics
106770 !SQ P16528 98-272 # ! Structural genomics target
106829 !SQ P77734 97-269 # ! Structural genomics target
111115 ! contains insert domain (140-229) of the Enolase N-terminal domain-like fold (scop_cf 54825)
106014 !SQ Q9WZV5 # ! Structural genomics target
55785 ! alpha-beta(2)-alpha(2)-beta(3)
86370 ! ultra-high resolution structure
40897 ! cryotrapped early light cycle intermediate
107839 !SQ P16113
40900 ! the p65 crystal form
105220 !SQ P16113
105221 !SQ P16113
40902 ! photostationary state: 50% ground state, 50% bleached
40904 ! dark state (unbleached)
86888 ! 1-25 deletion mutant
111118 ! Heme-regulated cyclic AMP phosphodiesterase; formerly hypothetical protein YddU
108455 !SQ P76129 12-124
105304 !SQ P76129 8-126
105302 !SQ P76129 8-126
108457 !SQ P76129 12-124
88853 ! contains PAC motif
103184 ! contains PAC motif
103185 ! endothelial pas domain protein 1, EPAS-1
93087 ! PAS-B domain; complexed with a lxxll motif peptide, chain B
75516 ! alpha(2)-beta(2)-alpha(2)-beta(3)-alpha; possibly related to the PAS domain
103190 ! alpha(2)-beta(2)-alpha(2)-beta(3); possibly related to the PAS domain
103192 ! citrate-binding domain
64356 ! beta(2)-alpha-beta(3)-alpha(2)
103196 ! alpha-beta(2)-alpha-beta(3)-alpha; structurally most similar to the SNARE-like superfamily with a circular permutation of the terminal helices
103197 ! Pfam 03259
90836 ! structural genomics
111120 ! remote homolog that forms the characteristic complex structures with other members 
105676 !SQ Q9UHA4
108553 !SQ O88653
108555 !SQ O88653
108554 !SQ Q9JHS3
105677 !SQ Q9JHS3
108556 !SQ Q9JHS3
111125 ! binds heme between the N-terminal 4-helical bundle and the C-terminal alpha-beta(2)-alpha-beta(2) subdomains
107678 !SQ Q8RBX6 1-188
107680 !SQ Q8RBX6 1-188
107672 !SQ Q8RBX6 1-188
109541 !SQ Q8RBX6 1-191
55796 ! alpha-beta-alpha-beta-alpha(2)-beta(2); 3 layers, alpha/beta/alpha; mixed sheet: order 1342
55798 ! groups mammalian SCP/TPX1; insects AG3/AG5; fungi SC7/SC14 and plant PR-1
105756 !SQ  Q9H4G4
55803 ! beta-alpha(2)-beta(3)-alpha(3); 3 layers, alpha/beta/alpha; mixed sheet: order 1342; loop crossing
64362 ! elaborated with additional secondary structures
55810 ! beta(2)-alpha-beta(3)-alpha; 3 layers: alpha/beta/alpha; mixed sheet ! contains beta-grasp motif
60188 ! CASP4
100768 ! structural genomics 
103200 ! gene Rv1700
100774 ! structural genomics 
100719 ! structural genomics 
100673 ! structural genomics 
71830 ! structural genomics
103214 ! duplication: consists of two structurally similar domains; the N-terminal domain has a rudiment Nudix fold, the C-terminal, probably catalytic, domain has the canonical fold
100852 ! structural genomics
104283 !SQ Q46822
104324 !SQ Q46822
104285 !SQ Q46822
95621 ! structural genomics
105123 !SQ P32056
55815 ! core: alpha-beta(2)-alpha-beta(2)-alpha-beta; 3 layers; mixed sheet: order 31425
103944 !SQ P07024 26-550
103954 !SQ P07024 26-550
103956 !SQ P07024 
55820 ! core: alpha-beta(2)-alpha-beta-alpha(2)-beta(2)-alpha-beta-alpha-beta; 3 layers; mixed twisted sheet of 7 strands; order 7126354; strands 7 and 1 are parallel to each other
55822 ! contains two additional strands in the C-terminal extension
40927 ! structural genomics
72103 ! structural genomics
71634 ! structural genomics
64372 ! contains one additional helix in the C-terminal extension
105822 !SQ Q60364
107115 !SQ Q5A3V6
107117 !SQ Q5A3V6
82770 ! beta(2)-alpha(2)-beta-alpha-(beta); strand 4 is very short; 3 layers; antiparallel (mixed) beta-sheet; order 312(4)
82773 ! intron-associated endonuclease 1
55825 ! core: alpha-beta-alpha-beta(2)-(alpha-beta)2-alpha-beta(2)-alpha-beta; 3 layers; bifurcated mixed sheet
55827 ! Pfam 04073
40929 ! structural genomics
40930 ! structural genomics
103220 ! annotated as putative DNA-binding protein
100809 ! structural genomics
108665 !SQ Q8U9M7 # ! Structural genomics target
55830 ! contains large mixed beta-sheet
105464 !SQ list: Q5CGA3 Q27552 # 100% Identity
69795 ! complex alpha+beta fold; contains antiparallel 5-stranded beta-sheet: order 12354
69799 ! TM0449
86569 ! structural genomics
86585 ! structural genomics
86581 ! structural genomics
86561 ! structural genomics
86577 ! structural genomics
86573 ! structural genomics
68794 ! structural genomics
86565 ! structural genomics
86589 ! structural genomics
55845 ! contains mixed beta-sheet
55847 ! Family 2 zinc amidase;
106102 !SQ Q9VYX7
105228 !SQ Q9VYX7 37-203
105664 !SQ Q96LB9 177-341
105663 !SQ Q96LB9 177-341
55855 ! beta-alpha-beta(2)-alpha(1,2)-(beta)-alpha(2)-beta; 3 layers: a/b/a; antiparallel beta-sheet, order: 1532(4)
103875 !SQ P00171 8-89
105542 !SQ P00171 7-88
62265 ! outer mitochondrial membrane cytochrome b5
61950 ! apo form
41083 ! apo form
41082 ! apo form
55862 ! a prokaryotic homologue of cytochrome b5
55864 ! C-terminal domain is beta/alpha barrel
90733 ! structural genomics
99063 ! structural genomics
55868 ! beta(2)-alpha-beta-(alpha)-beta(2); left-handed crossover between strands 2 & 3
55873 ! 8-stranded mixed beta-sheet; 2 layers: alpha/beta
41097 ! CASP2
108147 !SQ P07900 16-223
108132 !SQ P07900 16-223
108133 !SQ P07900 16-223
108142 !SQ P07900 16-223
108138 !SQ P07900 16-223
108137 !SQ P07900 16-223
108135 !SQ P07900 16-223
108134 !SQ P07900 16-223
108140 !SQ P07900 16-223
108136 !SQ P07900 16-223
108146 !SQ P07900 16-223
108139 !SQ P07900 16-223
108141 !SQ P07900 16-223
108148 !SQ P08238 10-220 # HSP 90-beta isoform
106757 !SQ P41148 76-285 # Endoplasmin, GRP94
107616 !SQ 
106747 !SQ P41148 76-285 # Endoplasmin, GRP94
106751 !SQ P41148 76-285 # Endoplasmin, GRP94
73373 ! complexed with clorobiocin
41106 ! novobiocin-resistant mutant complexed with novobiocin
82778 ! contains an H2TH domain inserted after this domain and before the second family-specific domain
61774 ! ATP-binding domain (p4) only
61776 ! ATP-binding domain (p4) only
61782 ! ATP-binding domain (p4) only
61778 ! ATP-binding domain (p4) only
61780 ! ATP-binding domain (p4) only
61783 ! ATP-binding domain (p4) only
106908 !SQ O32727
107001 !SQ O32727
106918 !SQ O32727
107008 !SQ O32727
104816 !SQ P06712 194-349
55889 ! core: alpha-beta-alpha-beta(2)-(alpha)-beta(2)
55890 ! Histidine kinase-like fold lacking the kinase ATP-binding site
55894 ! alpha+beta fold
107767 !SQ P23540
41121 ! CASP3
105536 !SQ P84146
64375 ! alpha+beta fold; could have evolved from a glucocorticoid receptor-like zinc finger domain
64377 ! some family sequences retain zinc-binding residues
60231 ! structural genomics
111147 ! beta(2)-alpha(3); contains zinc-less 'zinc finger'-like fold (scop_cf 57715; see also scop_cf 64375)
106196 !SQ Q9HU36
55903 ! complex alpha+beta motif
55908 ! duplication: composed of 5 alpha-beta(2)-alpha-beta units arranged around pseudo fivefold axis
55914 ! common fold is elaborated with many active site-forming insertions
64380 ! functionally related to the amidinotransferase, similar active sites
103232 ! functionally related to the amidinotransferase, similar active sites
111152 ! # functionally related to the amidinotransferase, similar active sites 
109245 !SQ Q9UM07
109242 !SQ Q9UM07
109239 !SQ Q9UM07
111155 ! functionally related to the amidinotransferase, similar active site
108687 !SQ Q8GWW7 # ! Structural genomics target
109495 !SQ Q9ZN18 # ! Structural genomics target
55919 ! duplication: composed of two very similar alpha+beta folds
80755 ! CASP5
55926 ! contains insert domain with a circularly permuted "winged helix" fold
55927 ! methionine aminopeptidase 2 contains insert domain with a circularly permuted "winged helix" fold
55930 ! duplication: common core consists of two beta-alpha-beta2-alpha repeats
104980 !SQ P51541
105425 !SQ P51541
111160 ! structural and functional relationships to Glutamine synthetase
104846 !SQ P77213 # ! Structural genomics target
107290 !SQ Q8ZR41 # ! Structural genomics target
55944 ! beta-alpha-beta(4)-alpha
55946 ! duplication: consists of two clear structural repeats
55947 ! structure of the N-terminal domain is not known yet
41279 ! complexed with DNA containing TATA-box
85695 ! a ternary complex with DNA and Brf1 peptide
55952 ! contains a single copy of this fold
104332 !SQ P04395
78286 ! borohydride trapped intermediate
78284 ! borohydride trapped intermediate
76724 ! borohydride trapped intermediate complex
78282 ! borohydride trapped intermediate
103239 ! contains a single copy of this fold
103243 ! contains a single copy of this fold
103244 ! Pfam 02149
108384 !SQ Q8C6G9 373-452 # ! Structural genomics target
103247 ! contains a single copy of this fold decorated with additional structures; forms dimer
103248 ! Pfam 03625; domain of unknown function DUF302
96315 ! structural genomics; MCSG target APC35924
103837 !SQ Q84BQ8 # ! Structural genomics target
64383 ! contains a single copy of this fold
59645 ! complexed with an FtsZ fragment
55957 ! contains a single copy of this fold and an extra beta-strand at the C-terminus
55961 ! contains a single copy of this fold with a alpha-beta2 insertion after the first helix; there is a cavity between the beta-sheet and the long C-terminal helix
71191 ! isoform llpr10.1a
71205 ! isoform llpr10.1b
100812 ! structural genomics
99075 ! complexed to phosphatidylcholine
100078 ! complexed to phosphatidylinositol
55969 ! contains a few insertion and C-terminal extension compared with Bet v1
107928 !SQ Q53122 17-451
107937 !SQ Q53122 17-451
109590 !SQ Q82XK1 ! Structural genomics target
111171 ! forms segment-swapped dimers further organized in hexamers
106555 !SQ P84137
55972 ! duplication: consists of 3 similar intertwined domains ! structural repeat: beta-alpha-beta(2)-alpha-beta; two layers, alpha/beta
55975 ! synonym: methionine adenosyltransferase, MAT
92690 ! complexed with both substrates ATP and methionine
55978 ! contains two helices and two beta sheets ! duplication: fold has internal pseudo two-fold symmetry
55980 ! duplication: consists of three domains of this fold
103997 !SQ P00583
55983 ! duplication: consists of two domains of this fold
41389 ! CASP1
106096 !SQ P15873
98068 ! complexed with a FEN-1 peptide, chain B
98036 ! complexed with a FEN-1 peptide, chain B
107775 !SQ Q975N2
106575 !SQ P16790 1-290
103255 ! duplication: consists of two beta(3)-alpha(2) structural repeats; single barrel-like beta-sheet 
100823 ! structural genomics
56002 ! beta(2)-alpha-beta-alpha-beta; 2 layers: a/b; mixed sheet: order 1243: crossing loops
56003 ! duplication: consists of 4 structural repeats arranged in 2 lobes ! contains one left-hand beta-alpha-beta unit per lobe
108742 !SQ Q46509
105584 !SQ Q46509
108446 !SQ P80457
106376 !SQ P72224
56013 ! beta-alpha-beta-alpha-beta(3)-alpha(2,3); mixed sheet: order 12345; left-handed crossover connection between strands 1 and 2
56014 ! duplication: contains two domains of this fold
56018 ! core: alpha(2)-beta(2)-alpha-beta; mixed sheet: order 213
56019 ! N- and C-termini undergo large conformational rearrangement upon ligand binding
70295 ! complex with mad1
68689 ! complex with MBP1 peptide
41449 ! "apo" form
56023 ! beta-alpha-beta-alpha-beta-alpha-beta(4)-alpha; mixed sheet: order 1765234
64391 ! duplication: contains two domains of this fold arranged as in the Nuc dimer
108221 !SQ P84147
108217 !SQ P84147
108215 !SQ P84147
108211 !SQ P84147
108223 !SQ P84147
108219 !SQ P84147
108213 !SQ P84147
85931 ! complexed with a topoisomerase I-derived peptide, chain C
104514 !SQ P38319 79-538
56028 ! corner-like structure formed by two sheets and filled in with 2-3 helices
56029 ! duplication: consists of two beta-alpha-(beta)-beta(2) motifs; some topological similarity to the ferredoxin-like fold
56030 ! note: the solution structure determinations disagree in the relative orientations of two motifs
41454 ! this structure is probably incorrect, as its secondary structure elements are loosely packed
56036 ! 3 layers: beta/beta/alpha sandwich
56041 ! 3 layers: alpha/beta/alpha; partial topological similarity to the ferredoxin-like fold
103260 ! duplication: tandem repeats of two PurM-like units arranged like the PurM subunits in the dimer 
103261 ! TM1246
100849 ! structural genomics
106387 !SQ P74881
103262 ! duplication: consists of two DCoH-like beta(2)-alpha-beta(2)-alpha structural repeats; 3 layers, beta/alpha/beta
98961 ! structural genomics; NESG target BR19
107945 !SQ P56122
107955 !SQ P56122
64396 ! 3 layers: beta/alpha/beta; buried helix
64398 ! forms strand-swapped dimer
69818 ! beta(2)-alpha-beta-alpha-beta(4); 3 layers: beta/alpha/beta; some similarity to the Hsp33 fold
67373 ! structural genomics
71584 ! structural genomics
68929 ! beta-alpha-beta(4)-alpha-beta(2); 3 layers: beta/alpha/beta; buried helix
82783 ! swapped dimer of beta(3)-alpha-beta(2)-alpha(2)-beta subunits; mixed beta-sheet; order: 321[4][5][6]; buried helix
92343 ! structural genomics
91110 ! structural genomics
90028 ! probably the same as YhfA
85013 ! structural genomics
108738 !SQ Q9X021 # ! Structural genomics target
103276 ! beta-alpha(4)-beta-alpha-beta; segregated alpha-helical and beta-sheet subdomains; dimeric beta-sheet barrel: n=6, S=10   
103280 ! structural genomics
56046 ! consists of 2 different alpha+beta subdomains arranged in a 4-layer structure: b/a/b/a
105145 !SQ P02361 ! complexed with the spc operon mRNA
56052 ! consists of two beta-sheets and one alpha-helix packed around single core
56055 ! duplication: consists of two domains of this fold
105324 !SQ P14135
41476 ! CA-atoms only
75552 ! consists of 2 different alpha+beta subdomains; forms subdomain-swapped dimers
70716 ! includes fragments of coiled coil domain
56058 ! Consists of two subdomains with different alpha+beta folds ! shares functional and structural similarities with the PIPK and protein kinase superfamilies
56068 ! subunit of acetyl-CoA and pyruvate carboxylases 
108703 !SQ Q9X0X7 # ! Structural genomics target
56076 ! duplication: CPS large subunit contains two full BC-like lobes: carboxyphosphate and carbamoyl phosphate domains
106330 !SQ P00968
56084 ! GTP-specific enzyme
56086 ! the common fold is interrupted by a 4-helical subdomain (residues 112-198)
41572 ! CASP1
56088 ! circularly permuted version of prokaryotic enzyme
56091 ! has a circularly permuted topology
56097 ! contains additional, N-terminal all-alpha subdomain
87664 ! complexed with the phosphorylated carboxyl-terminal peptide of RNA polymerase II, chains C and D
56103 ! consists of two alpha+beta subdomains
56104 ! shares functional and structural similarities with the ATP-grasp fold and protein kinase superfamilies
75558 ! TM1243
73018 ! structural genomics
109126 !SQ P23677 187-461
109120 !SQ P23677 187-461
109122 !SQ P23677 187-461
107475 !SQ P17105 203-458
56111 ! consists of two alpha+beta domains, C-terminal domain is mostly alpha helical
56112 ! shares functional and structural similarities with the ATP-grasp fold and PIPK
88854 ! members organized in the groups and subfamiles specified by the comments
88855 ! CMGC group; CDKs subfamily; serine/threonine kinase
76537 ! complex with cyclin and an 11-residue recruitment peptide from p27
76531 ! complex with cyclin and an 11-residue recruitment peptide from p53
103961 !SQ P24941
104390 !SQ P24941
108925 !SQ P24941
93285 ! complex with cyclin
108928 !SQ P24941
93291 ! complex with cyclin
93307 ! complex with cyclin
92945 ! complex with cyclin
103967 !SQ P24941
76525 ! complex with cyclin and an 11-residue recruitment peptide from retinoblastoma-associated protein
103949 !SQ P24941
93279 ! complex with cyclin
93301 ! complex with cyclin
76519 ! complex with cyclin and a 9 residue recruitment peptide from E2F
76543 ! complex with cyclin and an 11-residue recruitment peptide from p107
103289 ! CDK2 homologue Pfpk5
88857 ! CMGC group; CDKs subfamily; serine/threonine kinase
88859 ! CMGC group; CDKs subfamily; serine/threonine kinase
56129 ! CMGC group; ERK/MAPK subfamily; serine/threonine kinase
56132 ! CMGC group; ERK/MAPK subfamily; serine/threonine kinase
41652 ! phosphorylated
56134 ! CMGC group; ERK/MAPK subfamily; serine/threonine kinase
56137 ! CMGC group; ERK/MAPK subfamily; serine/threonine kinase
69823 ! CMGC group; GSK3 subfamily; serine/threonine kinase
104538 !SQ P49841 35-384
92691 ! complexed with axin peptide
56142 ! CMGC group; CK2 subfamily; serine/threonine kinase
56148 ! CMGC group; Clk subfamily; serine/threonine kinase
41679 ! residues 305-538 were deleted and replaced with Val-Asp
56116 ! AGC group; PKA subfamily; serine/threonine kinase
96230 ! complexed with peptide inhibitor, chain B
96229 ! complexed with peptide inhibitor, chain B
105757 !SQ P00517
96233 ! complexed with peptide inhibitor, chain B
106161 !SQ P00517
95955 ! triple mutant model of PKB; complexed with peptide inhibitor, chain B
95956 ! double mutant model of PKB; complexed with peptide inhibitor, chain B
95618 ! double mutant model of PKB; complexed with peptide inhibitor, chain B
97314 ! complexed with peptide inhibitor, chain B
82791 ! AGC group; RAC/Akt subfamily; serine/threonine kinase
90034 ! AGC group; GRKs subfamily; serine/threonine kinase
90036 ! AGC group; PBK subfamily; serine/threonine kinase
104006 !SQ O15530 75-363
104007 !SQ O15530 75-363
56120 ! CaMK group; CAMKI subfamily; serine/threonine kinase
56124 ! CaMK group; CAMKI subfamily; serine/threonine kinase
56126 ! CaMK group; CAMKI subfamily; serine/threonine kinase
75560 ! CaMK group; CAMKI subfamily; serine/threonine kinase
104063 !SQ P53355 2-285
56122 ! CaMK group; CAMKI subfamily; serine/threonine kinase
82789 ! CaMK group; MAPKAPK subfamily; serine/threonine kinase
64404 ! CaMK group; CAMKL subfamily; serine/threonine kinase
86268 ! complex with peptide, chain B
86269 ! complex with peptide, chain B
86267 ! complex with peptide, chain B
56146 ! OPK group; PAK/STE20 subfamily; serine/threonine kinase
82793 ! OPK group; PKN subfamily; serine/threonine kinase
56139 ! OPK group; CKI subfamily; serine/threonine kinase
90038 ! OPK group; AIRK subfamily; serine/threonine kinase
93310 ! complexed with a tpx2 peptide, chain B
103290 ! OPK group; RAF subfamily; serine/threonine kinase; possible evolutionary link to tyrosine kinases
56144 ! TKL group; STKR subfamily; serine/threonine kinase; possible evolutionary link to tyrosine kinases
108633 !SQ P36897 201-503
104389 !SQ P36897 200-500
56155 ! PTK group; Src subfamily; non-membrane spanning protein tyrosine kinase
56151 ! PTK group; Src subfamily; non-membrane spanning protein tyrosine kinase
41680 ! SH2 domain- and SH3 domain-binding regulatory tails are included
41684 ! SH2 domain- and SH3 domain-binding regulatory tails are included
56153 ! PTK group; Src subfamily; non-membrane spanning protein tyrosine kinase
75564 ! PTK group; Tec/Atk subfamily; non-membrane spanning protein tyrosine kinase
56164 ! PTK group; CSK subfamily; non-membrane spanning protein tyrosine kinase
56166 ! PTK group; Abl subfamily; non-membrane spanning protein tyrosine kinase
82797 ! PTK group; MUSK subfamily; non-membrane spanning protein tyrosine kinase
103292 ! PTK group; FAK subfamily; non-membrane spanning protein tyrosine kinase
82795 ! PTK group; EGFR subfamily; membrane spanning protein tyrosine kinase
69827 ! PTK group; Eph/Elk/Eck subfamily; membrane spanning protein tyrosine kinase
103294 ! PTK group; Eph/Elk/Eck subfamily; membrane spanning protein tyrosine kinase
64406 ! PTK group; Tie/Tck subfamily; membrane spanning protein tyrosine kinase
56158 ! PTK group; FGFR subfamily; membrane spanning protein tyrosine kinase
75562 ! PTK group; FGFR subfamily; membrane spanning protein tyrosine kinase
56160 ! PTK group; PDGFR/VEGFR subfamily; membrane spanning protein tyrosine kinase
103296 ! PTK group; PDGFR/VEGFR subfamily; membrane spanning protein tyrosine kinase
106397 !SQ P10721 547-935
106396 !SQ P10721 547-935
103298 ! PTK group; CSF-1/PDGF receptor subfamily; membrane spanning protein tyrosine kinase
56162 ! PTK group; InsR subfamily; membrane spanning protein tyrosine kinase
97761 ! complexed with adaptor protein Aps 
69825 ! PTK group; InsR subfamily; membrane spanning protein tyrosine kinase
103300 ! PTK group; HGFR subfamily; membrane spanning protein tyrosine kinase
111192 ! AGC group (?); S6 kinase subfamily; serine/threonine kinase
108971 !SQ O75582 24-345
111194 ! PTK group; Tec/Atk subfamily; non-membrane spanning protein tyrosine kinase 
105755 !SQ Q08881 357-619
105830 !SQ Q08881 357-619
105832 !SQ Q08881 357-619
111196 ! OPK group; WNK subfamily; serine/threonine kinase 
106421 !SQ Q9JIH7 211-480
111198 ! PTK group; SYK/ZAP-70 subfamily; non-membrane spanning protein tyrosine kinase 
107681 !SQ P43403 328-606 # structure of the N-terminal SH2 domains (1-132;133-256) is also known: 1m61 (scop_sp 89997)
111200 ! PTK group; Tck subfamily; non-membrane spanning protein tyrosine kinase 
107657 !SQ Q07912 117-389
107669 !SQ Q07912 117-389
107676 !SQ Q07912 117-389
111202 ! CMGC group; ERK/MAPK subfamily; serine/threonine kinase 
107913 !SQ P45983 9-363
107914 !SQ P45983 9-363
56168 ! Atypical protein kinases
64408 ! Atypical protein kinases
64409 ! contains closed beta-barrel (n=6; S=10) in the N-terminal subdomain
107227 !SQ O30245 # AF2426
107237 !SQ O30245 # AF2426
107241 !SQ O30245 # AF2426
56175 ! consists of two alpha+beta subdomains
109062 !SQ P56216
109066 !SQ P56216
109058 !SQ P56216
109070 !SQ P56216
56180 ! the other subunit is a short-chain cytochrome c
109072 !SQ Q9T0N8
109074 !SQ Q9T0N8
109076 !SQ Q9T0N8
109078 !SQ Q9T0N8
108447 !SQ P80457
106378 !SQ P72222
56193 ! consists of two alpha+beta subdomains
56196 ! N-terminal domain is a FAD-binding domain
56198 ! consists of two alpha+beta subdomains
56746 ! consists of two alpha+beta domains
56748 ! contains additional insert all-alpha subdomain
56203 ! consists of two alpha+beta domains; the N-terminal domain is array of helices and beta-hairpins; the C-terminal domain is an a/b sandwich with one left-handed beta-alpha(n)-beta unit; conformational flexibility of domain orientation
56208 ! 4 layers a/b/b/a; inside is a sandwich of two 2-stranded beta-sheets
56209 ! duplication: contains two structural repeats
56212 ! also <i>Rhodococcus sp.</i> R312
107831 !SQ Q7SID2
107835 !SQ Q7SID2
107837 !SQ Q7SID2
107833 !SQ Q7SID2
56213 ! beta-alpha(3)-beta(2) motif
56214 ! possibly related to the IspF </i>(<a href="../search.cgi?sccs=d.79.5">d.79.5</a>)<i> and YjgF-like superfamilies </i>(<a href="../search.cgi?sccs=d.79.1">d.79.1</a>)<i>
64418 ! forms trimers with three closely packed beta-sheets similar to the IspF trimers
59685 ! complexed with holo-ACP
56215 ! monomeric; tandem duplication of beta-alpha(3)-beta(2) motif
56218 ! contains beta-sandwich; duplication of alpha+beta motif
56223 ! Major apurinic/apyrimidinic endonuclease APE1
108898 !SQ P08547 2-237 # ! 94% sequence identity
105949 !SQ O06523 23-283
109287 !SQ Q93139 1-184
103310 ! heme-binding homologue of IPP5
56227 ! contains sandwich; duplication of alpha+beta motif with single mixed sheet ! motif: beta(2)-alpha-beta(3)-alpha-beta; strand order 216345, strands 1 and 6 are parallel
56234 ! 4 layers: alpha/beta/beta/alpha; has an unusual sheet-to-sheet packing
56235 ! N-terminal residue provides two catalytic groups, nucleophile and proton donor
56236 ! has slightly different topology than other families do
109583 !SQ P17169 1-238
109581 !SQ P17169 1-238
69831 ! Asparagine synthetase B homologue
103312 ! carbapenam synthetase CarA
106796 !SQ Q9I437
56245 ! also contains 2 all-alpha and a beta-barrel domains ! will be divided into domains in future release
41838 ! A slow processing precursor
77194 ! complex with glutarate
72370 ! Single-chain precursor structure
77193 ! complex with glutaryl-7-aminocephalosporanic acid
93444 ! single-chain precursor
56254 ! The structure of yeast proteasome complexed with the proteasome activator pa26 is available from PDB </i>(<a href="../pdb.cgi?pdb=1fnt">1fnt</a>)<i>. The 1FNT entry designates protein chains by both upper case and lower case letters creating problems with its processing and presentation in SCOP; the proteasome activator pa26 structure is classified elsewhere in SCOP </i>(<a href="../search.cgi?sccs=a.24.8">a.24.8</a>)<i>
41903 ! different sequences
41889 ! different sequences
41917 ! different sequences
71351 ! different sequences
95931 ! contains unprocessed pro-peptides
56255 ! contains an extension to the common fold at the N-terminus
84028 ! alpha-ring only
56257 ! The structure of yeast proteasome complexed with the proteasome activator pa26 is available from PDB </i>(<a href="../pdb.cgi?pdb=1fnt">1fnt</a>)<i>. The 1FNT entry designates protein chains by both upper case and lower case letters creating problems with its processing and presentation in SCOP; the proteasome activator pa26 structure is classified elsewhere in SCOP </i>(<a href="../search.cgi?sccs=a.24.8">a.24.8</a>)<i>
41959 ! different sequences
41945 ! different sequences
41973 ! different sequences
71372 ! different sequences
56258 ! dodecameric prokaryotic homologue of proteasome
56262 ! the precursor chain is cleaved onto 2 fragments by autoproteolysis
87773 ! precursor D151N mutant
42009 ! Precursor W11F mutant
87782 ! precursor D151N mutant
42011 ! Precursor of the T152C mutant
42015 ! Precursor T152A mutant
103315 ! isoaspartyl peptidase with L-asparaginase activity ! putative L-asparaginase YbiK
106362 !SQ P37595
75569 ! has a putative active site in the same topological location as the Ntn hydrolase but lacks the N-terminal nucleophile
73019 ! structural genomics
56265 ! duplication of beta(3)-alpha-beta-alpha motif; 4 layers: alpha/beta/beta/alpha
56266 ! convergent similarity to the Ntn amidohydrolases
56267 ! Pfam 03576
111219 ! contains extra C-terminal alpha+beta domain [beta-alpha(2)-beta(2)-alpha-beta(2); 2 layers, a/b; mixed beta-sheet, order: 51423, strands 1 and 4 are parallel to each other]
111221 ! d1: 8-260; d2: 261-390
108950 !SQ Q53940
108958 !SQ Q53940
108954 !SQ Q53940
56270 ! duplication of beta-alpha-beta(2) motif; 4 layers: alpha/beta/beta/alpha; contains "silk" beta-sandwich
56271 ! two chains result from self-processing single-chain precursor; form heterohexamer
85283 ! the proenzyme S53A mutant
56275 ! duplication of beta-alpha-beta(4)-alpha-beta-alpha-beta(2) motif; 4 layers a/b/b/a; antiparallel beta-sheets: order 23451687
63156 ! self-processing ester intermediate
85095 ! S68A proenzyme processing mutant
111222 ! homodimer; the subunit fold and assembly are similar to those of the structural repeats of the eukaryotic enzyme
107140 !SQ Q9WZC3
107152 !SQ Q9WZC3
56280 ! duplication of beta(4)-alpha-beta-alpha motif; 4 layers a/b/b/a; mixed beta-sheets
103846 !SQ P04190 31-257
100826 ! structural genomics
108896 !SQ Q9WZL4 # ! Structural genomics target
104089 !SQ list: Q841S6 Q693X1 Q93SP1 # 100% Identity
81607 ! 4 layers: alpha/beta/beta/alpha; antiparallel beta sheets
81606 ! contain binuclear metal (Mn) centre
56299 ! 4 layers: alpha/beta/beta/alpha; mixed beta sheets; contains duplication
56302 ! also contain an Ig-like domain
64427 ! contains C-terminal alpha/beta subdomain
105369 !SQ Q8U1N9
103945 !SQ P07024 26-550
103955 !SQ P07024 26-550
103957 !SQ P07024 
107631 !SQ P36873 
105316 !SQ P37140 1-308
105376 !SQ P53041 176-499
80675 ! structural genomics; pfu-1218608
103320 ! similar to purple acid and protein phosphatases
99324 ! structural genomics
105244 !SQ Q58346 # ! Structural genomics target 
105242 !SQ Q58346 # ! Structural genomics target 
105246 !SQ Q58346 # ! Structural genomics target 
106019 !SQ P76495 # ! Structural genomics target
56316 ! 4 layers: alpha/beta/beta/alpha; mixed beta sheets; contains duplication
56317 ! Pfam 00795; some topological similarities to the metallo-dependent phosphatases and DNase I-like nucleases
107809 !SQ P60327
107813 !SQ P60327
107811 !SQ P60327
107807 !SQ P60327
64437 ! 4 layers: alpha/beta/beta/alpha; mixed beta sheets
106664 !SQ P84138 # ! Structural genomics target
105105 !SQ Q9K0A8
105111 !SQ Q8Z4J1
109536 !SQ Q83K13 # ! Structural genomics target
107542 !SQ Q83K13 # ! Structural genomics target
109585 !SQ Q9AAV3 # ! Structural genomics target
56321 ! duplication: contains four repeats of alpha-beta(2)-beta motif arranged in a 4 layer core structure: alpha/beta/beta/alpha; orthogonally packed beta-sheets
56322 ! the active site is formed by additional structures inserted into the core structure
69838 ! Aminodeoxychorismate synthase
111248 ! 4 layers: a/b/b/a; antiparallel beta sheets; similarities to ferredoxin-like fold (scop_cf 54861) in the N-terminal part (1-120) and to the Bacterial S-adenosylmethionine decarboxylase subunit (scop_fa 997656) in the C-terminal part (121-340)
111250 ! Pfam 01950
107956 !SQ Q975V5
56326 ! unusual fold, defines family
56328 ! N-terminal domain is NAD-binding module (alpha/beta Rossmann-fold domain)
82806 ! identical sequence to that from the <i>Thermus flavus</i> enzyme
108115 !SQ P80040
108119 !SQ P80040
108103 !SQ P80040
108107 !SQ P80040
108111 !SQ P80040
103991 !SQ O08349
103989 !SQ O08349
90050 ! family 4 glycosyl hydrolase 
90052 ! TM1834
100834 ! structural genomics
107742 !SQ P54716
105315 !SQ P84135
107991 !SQ Q9X108
56348 ! core: alpha3-beta3-alpha4; one side of beta-sheet is exposed
105079 !SQ P11387 203-767
105076 !SQ P11387 203-765
82807 ! consists of seven alpha-helices and three-stranded beta-sheet
82810 ! binds to fully methylated and hemimethylated GATC sequences at oriC
103834 !SQ P36658 71-181
56365 ! consists of four alpha-helices and three beta-ribbons
93847 ! complexed with DNA
64448 ! consists of four alpha-helices and two beta-hairpins
68125 ! a segment-swapped dimer
74358 ! complexed with a phospho-peptide from skap-hom
75573 ! consists of six alpha-helices and two beta-hairpins
56370 ! contains mixed beta-sheet
56379 ! (almost) identical with the anti-tumor and anti-HIV-1 protein MAP30
56382 ! different sequence variants
104317 !SQ P81446 1-249 # 89% sequence identity
104314 !SQ P81446 1-249 # 89% sequence identity
106855 !SQ Q6ITZ3 1-240
104104 !SQ Q6ITZ3 1-240
83285 ! X-ray derived abrin-based sequence
103333 ! seed isoform
56398 ! unusual fold
42248 ! one domain only
56412 ! duplication: consists of two domains of this fold, the second of which is catalytic
82812 ! mammalian-targeted relative of VIP2; C-terminal domain is catalytic, N-terminal domain interacts with Ib (binding component)
108177 !SQ P15879 41-251
69845 ! includes an all-alpha insert subdomain
95249 ! complexed with small molecule inhibitor 
95237 ! complexed with small molecule inhibitor 
95261 ! complexed with an optimized peptide substrate (chains C and D) in the presence of zinc
95255 ! complexed with an optimized peptide substrate (chains C and D) in the presence of zinc
95243 ! complexed with small molecule inhibitor 
82814 ! the two disulfide bridges and N-terminal alpha helices are characteristic for all ecto-ARTs
82815 ! NAD glycohydrolase and auto-ADP-ribosylation activity
107904 !SQ P09874 661-1010
111257 ! shares the common structural core with other families; unknown function
105222 !SQ Q9K2L5 29-204
56419 ! alpha-beta(5)-alpha; 3 layers: a/b/a; meander beta-sheet wraps around the C-terminal alpha-helix
56420 ! nickel-dependent enzyme
74230 ! complexed with antibiotic actinonin
42306 ! incorrect model(?)
90713 ! complexed with antibiotic actinonin
74231 ! complexed with antibiotic actinonin
104480 !SQ Q9F4L4
74212 ! complexed with antibiotic actinonin
69847 ! unusual fold
56424 ! unusual fold
56432 ! contains additional N-terminal multiheme domain
56435 ! unusual fold
56437 ! Pfam 00059
90059 ! major protein of the eggshell calcified layer
88861 ! heterodimeric coagulation factors IX/X-binding protein (IX/X-BP)
71235 ! complexed with the von Willebrand factor a1 domain
99282 ! complexed with the von Willebrand factor a1 domain
108406 !SQ Q7T2Q1 24-157
88867 ! heterodimeric coagulation factors IX/X-binding protein (IX/X-BP)
71236 ! complexed with the von Willebrand factor a1 domain
99283 ! complexed with the von Willebrand factor a1 domain
108407 !SQ Q7T2Q0 27-153
105710 !SQ Q9NNX6 219-397 # 1SL6 also contains two repeats of neck; shorter fragments (253-384) for each 1SL4 and 1SL5
105711 !SQ Q9NNX6 219-397 # 1SL6 also contains two repeats of neck; shorter fragments (253-384) for each 1SL4 and 1SL5
105717 !SQ Q9NNX6 219-397 # 1SL6 also contains two repeats of neck; shorter fragments (253-384) for each 1SL4 and 1SL5
56456 ! also contains EGF-like module
65102 ! complexed with psgl-1 peptide
42420 ! CASP3
56465 ! trimeric plasminogen binding protein with an alpha-helical coiled coil
104963 !SQ P05452 85-202
106785 !SQ P07897 1912-2037
109425 !SQ Q7M462
109421 !SQ Q7M462
56474 ! an enteropathogenic serotype
103353 ! contains extra N-terminal beta-strand and C-terminal beta-hairpin
56480 ! decorated with many insertions in the common fold
75585 ! duplication: consists of two subdomains of this fold; segment swapping within and between individual domains
73909 ! alpha 1 (chains A,B,D and E) and alpha 2 (chains C and F) isoforms
106540 !SQ P02462 1445-1667 # 98% sequence identity
106528 !SQ P02462 1445-1667 # 98% sequence identity
78556 ! alpha 1 (chains A,B,D,E,G,H,J and K) and alpha 2 (chains C,F,I and L) isoforms
111264 ! unusual fold
108503 !SQ Q868M7 11-442
56486 ! unusual fold; disulfide-rich; core: beta-x-alpha-beta-loop-beta
56488 ! has some structural similarity to the long-chain scorpion toxins
103888 !SQ P05981 50-159
103886 !SQ P05981 50-159
56495 ! unusual fold
42456 ! CASP2
104899 !SQ P02679
104909 !SQ P02679
104897 !SQ P02675
104907 !SQ P02675
56501 ! unusual fold
56506 ! unusual fold; core: beta-alpha(2)-beta(2)-alpha(2)-beta-alpha-beta; antiparallel beta-sheet: order 12354
71599 ! structural genomics
90063 ! unusual fold; core: beta(2)-loop-beta(2)-alpha-beta; mixed beta-sheet: order 51243; parallel strands 2 and 4
86557 ! structural genomics
81661 ! unusual fold; core: beta-alpha(2)-beta(3)-alpha(2)-beta(2); 6-stranded antiparallel beta-sheet, order: 165432
106475 !SQ P04191
108582 !SQ P04191
106479 !SQ P04191
75860 ! Structure in the absence of calcium ions
75894 ! Structure in the e2 state
104524 !SQ Q6PIE5 384-590 # 98% sequence identity
111270 ! minimal fold of this domain: 
107728 !SQ P03960 316-451
106049 !SQ P03960 316-451
109492 !SQ P03960 316-451
103358 ! unusual fold; bifurcated beta-sheet; left-handed beta-alpha-beta unit
56511 ! unusual fold
108468 !SQ P29477 77-495
108469 !SQ P29476 298-716
105090 !SQ P29476
105088 !SQ P29476
105094 !SQ P29473 67-482
105092 !SQ P29473 67-482
56518 ! unusual fold
56520 ! contains an insert subdomain of ClpS-like fold
56521 ! the insert subdomain (residues 93-183) is usually disordered in the structures
97700 ! the insert subdomain is fully ordered
42562 ! CA-atoms only
82824 ! the insert subdomain (residues 168-239) is fully ordered
56523 ! unusual fold; contains 3 layers of beta-sheet structure and a beta-grasp like motif
56528 ! unusual fold; contains 3 layers of beta-sheet structure
86122 ! structural genomics
64459 ! duplication: tandem repeat of two FAH domains
103867 !SQ P53889 # ! Structural genomics target
106047 !SQ P77608 # ! Structural genomics target
56533 ! unusual fold
56541 ! unusual fold
106193 !SQ P13702 4-377 # chain B coverage
69863 ! unusual fold
108715 !SQ Q9X2A1 # ! Structural genomics target
103364 ! complex alpha+beta fold; contains a region of similarity to the ferredoxin-like fold
99162 ! structural genomics
82828 ! consists of two different alpha+beta domains
82831 ! characterized as tRNA-Ile-lysidine synthetase, TilS
90072 ! consists of two different alpha+beta subdomains; 2 zinc-binding sites
90073 ! DNA-binding domain
56547 ! unusual fold
56552 ! unusual fold; contains a left-handed beta-alpha-beta unit
105787 !SQ Q9Z9H6 #! part of multichain biological unit
56557 ! unusual fold; trimer
88873 ! unusual fold; trimer
88876 ! intertwinned homotrimer; subdivided into the neck, collar, head and bonnet regions
83059 ! neck and collar regions only
56562 ! unusual fold
64464 ! unusual fold
103369 ! unusual fold; intertwined dimer; consists of two different structural domains
111277 ! alpha(2)-beta(2)-alpha-beta-alpha-beta(2)-alpha; 2 layers: a/b; antiparallel beta-sheet: order 21354; strands 1,3 and 5 and the C-terminal helix are longer than other secondary structures
111278 ! the dimer, formed in the crystals, is a probable biological unit 
107127 !SQ Q9UX16 # ! Structural genomics target
111282 ! consists of two different alpha+beta domains; d1: [duplication of alpha-beta(3)-alpha motif; 2 layers: a/b; antiparallel beta-sheet, order: 321456; strands 1, 2, 4 and 5 are twice longer than other secondary structures]; d2 [ complex fold; contains beta-barrel (n=5, S=10)]
111286 ! d1: 1-214; d2: 215-433
108719 !SQ Q9WZI6 # ! Structural genomics target
56567 ! not a true fold
56568 ! not a true superfamily
56569 ! consists of a long beta-hairpin and a single alpha-helix
67488 ! extended conformation wrapped around the secretion chaperone SicP
90077 ! beta-hairpin and a short alpha-helix bound to the core subunits
90079 ! there are other PDB entries with lower resolution structures of the Ubiquinol-cytochrome c reductase complex, in which this subunit has incomplete and probably mistraced structure that is not classified in scop
104280 !SQ P13272
104250 !SQ P13272
105903 !SQ P13272 1-57
56573 ! contains a cluster of helices and a beta-sandwich
42624 ! intact, in the delta conformation (partial loop insertion)
42628 ! intact chain: a canonical template for active serpins
42629 ! complex with trypsin
93404 ! complexed with trypsinogen
61117 ! intact chain
76975 ! intact chain
93376 ! intact chain in the native conformation
42635 ! cleaved polymer
42634 ! intact chain
42636 ! intact chain
42637 ! intact chain
106738 !SQ P01008
84621 ! complexed with peptides, chains C and D
84233 ! complexed with peptides, chains C and D
105952 !SQ P01008
63256 ! deletion mutant complexed with peptide mimicking the reactive center loop, chain P
66771 ! cleaved form
64470 ! Michaelis serpin-trypsin complex
68356 ! Michaelis serpin-trypsin complex
91235 ! cleaved form
42676 ! cleaved form
42677 ! cleaved form
90080 ! Serpin from a thermophilic prokaryote
85107 ! structural genomics
56595 ! contains a cluster of helices and a beta-sandwich
56600 ! contains a cluster of helices and an alpha+beta sandwich
104340 !SQ P15555
105423 !SQ P15555 34-378
104338 !SQ P15555
104339 !SQ P15555
104334 !SQ P15555
104337 !SQ P15555
74437 ! ultra high resolution structure
77969 ! TEM-34 variant
77968 ! TEM-32 variant
71922 ! TEM-64 variant
77967 ! TEM-30 variant
42699 ! acyl-enzyme intermediate
56609 ! inhibited by tazobactam
104501 !SQ P14557 22-286
108875 !SQ P14557 22-286
90082 ! almost identical sequence to SHV-1
42707 ! circularly permuted
42718 ! omega loop deletion mutant (residues 163-178 deleted)
42726 ! CA-atoms only
56617 ! imipenem-hydrolyzing
56618 ! contains small alpha+beta subdomain inserted in the common fold
104502 !SQ P05364 22-381
103375 ! closely related to class D beta-lactamase
42771 ! CA-atoms only
107361 !SQ Q53613 21-383 # ! Structural genomics target
109532 !SQ P18357 338-583
109534 !SQ P18357 334-581
90084 ! Pfam 04960
84995 ! structural genomics
107695 !SQ P77454
103377 ! consists of an all-alpha and alpha+beta domains 
99046 ! structural genomics
103382 ! contains a helical bundle with a buried helix and an alpha+beta insert domain
103387 ! consists of an all-alpha and alpha+beta domains connected by antiparallel coiled coil
56628 ! contains a cluster of helices and an alpha/beta domain
56633 ! contains an (8,10) beta-barrel and an all-alpha domain
56642 ! contains additional flavodoxin-like domain at C-terminus
56644 ! 2 domains: (1) all-alpha: 5 helices; (2) contains an open beta-sheet barrel: n*=5, S*=8; complex topology
56645 ! flavoprotein: binds FAD; constituent families differ in the numbers of C-terminal domains (four-helical bundles)
106718 !SQ P11310 34-421
103396 ! involved in biosynthesis of methoxymalonyl extender unit of fk520 polyketide immunosuppressant
105586 !SQ Q92947
105588 !SQ Q92947
56654 ! N-terminal domain is an alpha+beta, C-terminal domain is an alpha/beta with mixed beta-sheet
56666 ! MJ0109 ! structural genomics
103398 ! PH1897
100570 ! structural genomics
56670 ! sequence identical to that of <i>Saccharomyces cerevisiae</i>
64475 ! enzyme displaying both inositol-polyphosphate 1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities
90087 ! similar to the other family in overall domain architecture but each domain has a permuted topology
85739 ! structural genomics
56671 ! divided into morphological domains including "palm", "thumb" and "fingers"; the catalytic "palm" domain is conserved to all members
56672 ! "palm" domain has a ferredoxin-like fold, related to that of an adenylyl cyclase domain
107665 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107655 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107659 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107661 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107663 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107756 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107754 !SQ Q5KWC1 299-878 # 99% sequence identity; Geobacillus kaustophilus TaxID:1462
107075 !SQ P00581
107087 !SQ P00581
107064 !SQ P00581
107080 !SQ P00581
105707 !SQ P00581
105704 !SQ P00581
105685 !SQ P00581
105695 !SQ P00581
105688 !SQ P00581
105701 !SQ P00581
100888 ! contains a distinct 'fingers' domain possibly related to the C-terminal subdomain of hypothetical protein Ta1206 (1qw2)
62581 ! "palm" and "fingers" domains only
106366 !SQ Q9UNA4
106704 !SQ Q9UBT6 71-517
43015 ! fragment of "palm" and "fingers" domains
61845 ! fragment of "palm" and "fingers" domains
85323 ! fragment of "palm" and "fingers" domains
43017 ! fragment of "palm" and "fingers" domains
43020 ! fragment of "palm" and "fingers" domains
43018 ! fragment of "palm" and "fingers" domains
43022 ! fragment of "palm" and "fingers" domains
105112 !SQ P03355 RE 144-594 ! 'full length enzyme' fragment
43025 ! fragment of "palm" and "fingers" domains
43106 ! less ordered regions are modeled as poly-ALA
105207 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
105216 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
105213 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
105219 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
104678 !SQ P03366 186-725 # chain A coverage; chain B coverage: 156-584
107349 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595
105210 !SQ P04585 158-698 # chain A coverage; chain B is shorter: 159-595 
56692 ! multidomain; mostly alpha
79427 ! elongation complex; shows dramatic conformational changes in the transition from initiation to elongation transcription
43110 ! promoter complex
43111 ! initiation complex
76628 ! elongation complex; shows dramatic conformational changes in the transition from initiation to elongation transcription
104879 !SQ P03300 1748-2208
104880 !SQ P03300 1748-2208
107235 !SQ P03300 1748-2208
104881 !SQ P03300 1748-2208
107545 !SQ Q9QCE4 1858-2327
109434 !SQ Q9QCE4 1858-2327
82841 ! contains additional N-terminal domain (res. 1-380) and C-terminal "bracelet" domain (res. 891-1267)
79935 ! elongation complex with four phosphodiester bonds formed
79958 ! elongation complex with one phosphodiester bond formed
79804 ! initiation complex
64483 ! Multidomain subunits of complex domain organization
64484 ! The catalytic site is formed by the association of two double-psi beta-barrel domains, one from each subunit
105788 !SQ Q8RQE9 #! part of multichain biological unit
105789 !SQ Q8RQE8 #! part of multichain biological unit
81299 ! 3 domains: (1&2) alpha+beta, with domain 2 being inserted in domain 1; (3) all-alpha
81298 ! Domain 1 has topological and active site similarity to the Nucleotidyltransferases (eg. 1kny N-domain); domain 3 binds calmodulin
69887 ! decorated with many insertions and the C-terminal domain
105667 !SQ P40136
56711 ! 4 domains: (1) Toprim alpha/beta; (2&4) "winged helix"-like; (3) barrel: n=6, S=8
56712 ! duplication: the protein chain passing through the domains 2-4 makes two structural repeats ! The active site is formed by the toprim and "winged helix" domains (domains 1 and 4); these two domains are also found in the type II topoisomerase (DNA gyrase A) and in the alpha subunit of topoisomerase IV
56713 ! domain 4 contains the catalytic tyrosine residue
43237 ! 2nd and 3rd domains
43240 ! 2nd and 3rd domains
56718 ! 4 domains: (1) toprim alpha/beta; (2) "winged helix"-like; (3) alpha+beta; (4) all-alpha
56720 ! domain 2 contains the catalytic tyrosine residue
56721 ! the N-terminal fragment is homologous to known structure of DNA gyrase B
43251 ! fragment lacking toprim domain 1
56725 ! 2 domains: (1) toprim alpha/beta; (2) "winged helix"-like
56727 ! domain 2 contains the catalytic tyrosine residue
56730 ! 2 domains: (1) alpha+beta; (2) toprim alpha/beta
111303 ! consists of three domains: alpha-helical dimerisation domain (res. 1-53) with HhH motif (Pfam 00633); 'treble cleft' C4 zinc-finger domain (54-76; Pfam 02132); and Toprim domain (76-199; segment-swapped dimer; Pfam 01751)
108522 !SQ Q9ZNA2
56740 ! 2 domains: alpha+beta and all-beta
105080 !SQ P11387 203-767
105077 !SQ P11387 203-765
56751 ! 2 domains: (1) alpha+beta: beta3-alpha2-beta2; (2) alpha/beta, a part of its mixed sheet forms barrel: n=6, S=8
56755 ! domain 1: 1-120; domain 2: 121-277
56758 ! domain 1: 4-126; domain 2: 137-308
56761 ! 3 domains: (1) all-alpha; (2&3) alpha+beta
56769 ! 2 domains: (1) alpa/beta; (2) Fe-S cluster-bound
56795 ! 2 domains: (1) alpha/beta of a Rossmann-fold topology, binds NAD (2) multihelical array
105523 !SQ P07547
43348 ! complexed with carbaphosphonate, NAD+ and Zn2+
69895 ! TM0423
68790 ! structural genomics
86592 ! structural genomics; high-resolution structure
100668 ! structural genomics; high-resolution structure
103974 !SQ Q46856 # ! Structural genomics target
105082 !SQ P11549 # ! Structural genomics target
108833 !SQ Q9WZS7 # ! Structural genomics target
75614 ! 2 domains: (1) alpha+beta, 2 layers; (2) 3/4-helical bundle, right-handed twist, left-handed superhelix
75617 ! involved in siroheme synthesis
56800 ! 4 domains: (1&2) duplication: share the same alpha/beta fold; (3) beta-barrel; (4) alpha+beta
108276 !SQ Q6L8F0 # ! Structural genomics target
108278 !SQ Q6L8F0 # ! Structural genomics target
107940 !SQ Q6L8F0 # ! Structural genomics target
106449 !SQ Q8GN86
106435 !SQ Q8GN86
56807 ! 2 domains: (1) alpha+beta; (2) alpha/beta (interrupts domain 1)
79710 ! complex with a 23S rRNA fragment
75619 ! 4 domains: (1) 3-helical bundle; (2) alpha+beta of ferredoxin-like fold (3 and 4) alpha+beta of dsRDB-like fold
105046 !SQ Q9X183 
75624 ! 3 domains: (1) 3-helical bundle; (2 and 3 ) alpha+beta of different folds: domain 3 has a ferredoxin-like fold and is inserted in domain 2
72823 ! structural genomics
73885 ! structural genomics
79557 ! structural genomics ! CASP5
75631 ! 3 domains: (1) 4-helical bundle; (2) alpha+beta; (3) "winged helix"-like
56814 ! 3 domains: (1 and 2) alpha+beta; (3) mostly alpha, inserted in domain 2
79414 ! complexed with an N-terminal peptide of sed5p, chain B
56820 ! 3 domains: (1) spectrin repeat-like 3-helical bundle; (2 and 3) alpha/beta: Rossmann-fold topology
56822 ! contains extra N-terminal 3-helical bundle domain
82852 ! 4 domains: structures and assembly of domains 1 and 2 are similar to those of domains 1 and 3 of the CODH subunit; (3 and 4) alpha+beta
90095 ! 3 domains: (1) protozoan pheromone-like alpha-helical bundle; (2) rubredoxin-like domain lacking metal-binding site; (3) alpha+beta heterodimerisation domain: alpha-beta(5)-alpha
83849 ! domain boundaries: A:7-62;63-116;117-281, C:5-62;63-116;117-277
83850 ! domain boundaries: B:2-46;47-88;89-271, D:2-46;47-88;89-271
56825 ! 2 domains: (1) alpha-helical bundle; (2) beta-barrel (n=5, S=8)
64517 ! 3 domains: (1) alpha-helical bundle; (2&3) complex all-beta folds
62611 ! F41 fragment
99190 ! full-length flagellin
103408 ! 2 closely associated domains: (1) all-alpha, EF-hand like; (2) alpha+beta, Frataxin-like
111320 ! 2 domains; d1: [all-alpha; 3-helical bundle, similar to the immunoglobulin/albumin-binding domain-like fold (scop_cf 46996)]; d2: [alpha/beta; 3 layers, a/b/a; 6-stranded mixed beta-sheet, order: 321456, strand 6 is antiparallel to the rest]
111322 ! Pfam 01937
111324 ! d1: 36-117; d2: 118-365
109584 !SQ Q949P3 # ! Structural genomics target
111325 ! 3 domains; d1: alpha+beta [alpha(2)-beta(3); mixed sheet: 213]; d2: alpha/beta of the NAD(P)-binding Rossmann-fold superfamily (scop_sf 51735, most similar to scop_fa 51883 and scop_fa 51736); d3: alpha+beta of the glutamine synthetase/guanido kinase fold (scop_cf 55930); d1 and d3 form a single beta-sheet
111329 ! d1:4-138; d2:135-350; d3: 351-557
108066 !SQ P25080
108068 !SQ P25080
109080 !SQ P25080
111330 ! 2 domains: d1 [alpha/beta; related to the PFK N-terminal domain (scop_sf 53784)]; d2 [all-beta; atypical beta-sandwich made of 4 structural repeats of beta(3) unit]
111334 ! d1:1-96; d2:101-227
106030 !SQ O30297
111335 ! d1:5-132; d2:140-275
107568 !SQ O33196
107564 !SQ O33196
111336 ! 2 domains; d1 (1-64,174-335) [alpha/beta; 3 layers, a/b/a; mixed beta sheet of 9 strands, order: 219863457; strands 1, 5 and 8 are antiparallel to the rest]; d2 (65-142) [all-beta; barrel, closed (n=6, S=10); greek-key; topologically similar to the split barrel fold (scop_cf 50474)
108697 !SQ Q9WZ44 # ! Structural genomics target
111341 ! 2 domains; (1) alpha+beta (res 1-192), a circularly permuted rS5 domain 2-like fold (scop_cf 54210); (2) alpha/beta with parallel beta-sheet of 4 strands, order 2134 
105959 !SQ O29535
111346 ! consists of two domains; d1: alpha+beta (78-190; alpha-beta(4)-alpha-beta-alpha; 3 layers; antiparallel beta-sheet of 5 strands; order 51234); d2: alpha/beta similar to the G-domain fold (191-381; scop_fa 52592)
105970 !SQ P47736 ! chain D is disordered in the crystal
69902 ! 2 domains: (1) all-alpha, (2) alpha+beta; asymmetric homodimer with each domain intertwining with its counterpart
69905 ! non-structural RNA-binding protein
69907 ! 4 domains: three intertwined predominately alpha domains and one jelly-roll beta-sandwich
56830 ! large protein without apparent domain division; has a number of all-alpha regions and one all beta domain near the C-end
82855 ! large protein without apparent domain division
103416 ! large protein without apparent domain division
56836 ! multi-helical domains of various folds which is thought to unfold in the membrane
56838 ! contains "globin-like fold" with additional N-terminal and C-terminal helices
56841 ! contains an additional N-terminal a+b domain with six-stranded meander b-sheet
56843 ! the first ~450 residues are organized in coiled-coil structures
56847 ! contains globin-like fold with two additional helices at N-termini but has no counterpart to the first globin helix (A)
56850 ! seven-helical bundle with central helix surrounded by six others
56854 ! PROVISIONAL CLASSIFICATION, based on structural similarity to the diphtheria toxin domain
60286 ! isoform 1
60575 ! isoform 2
43394 ! complex with peptide from Bad (CH B)
94986 ! complexed with bim peptide, chain B 
107453 !SQ P41958 74-237 ! complexed with the activator egl-1 peptide (SQ O61667 48-76), chains C and D
56866 ! six-helical domain
81322 ! core: up-and-down bundle of seven transmembrane helices tilted 20 degrees with respect to the plane of the membrane
56871 ! a light-driven proton pump
86526 ! L intermediate
78344 ! K intermediate
78346 ! M1 intermediate
68580 ! a "mock-trapped" early-M intermediate
68579 ! an early-M intermediate
76865 ! ground state
43413 ! M intermediate structure (A) superimposed on the ground state structure (B)
43419 ! M intermediate trapped at 100K
76908 ! K intermediate
43417 ! L intermediate
73402 ! a solution structure
105372 !SQ P02945 17-245
105373 !SQ P02945 17-245
56874 ! a light-driven chloride pump
81320 ! Individual TM segments have a number of kinks and distortions
107234 !SQ P02699
66645 ! dark adapted
81407 ! not a true fold
81485 ! synonym: blastochloris viridis 
107962 !SQ P11846
81404 ! function unknown, probably acts as a regulator or is required for the assembly
81409 ! probably responsible for the dimerization of the mitochondrial cytochrome c oxidase
81413 ! function unknown, probably acts as a regulator or is required for the assembly
81417 ! function unknown, probably acts as a regulator or is required for the assembly
81421 ! function unknown, probably acts as a regulator or is required for the assembly
81425 ! function unknown, probably acts as a regulator or is required for the assembly
81429 ! function unknown, probably acts as a regulator or is required for the assembly
81467 ! interacts with subunit I and III, function unknown, non-essential for the enzymatic activity
81471 ! functionally important, corresponds to the first helix of the aa3 type subunit II absent in the ba3 type subunit II
73509 ! dimerisation domain only
104274 !SQ P00125
104244 !SQ P00125
105897 !SQ P00125
104276 !SQ P13272 # precursor of chains I,E and V,R
104246 !SQ P13272 # precursor of chains I,E and V,R
105899 !SQ P13272 79-274
81506 ! together with cytochrome b binds to ubiquinone
104278 !SQ P13271
104248 !SQ P13271
105901 !SQ P13271 #SP
81512 ! interacts with cytochrome c1 and ISP
104281 !SQ P00130
104251 !SQ P00130
105904 !SQ P00130
81516 ! the smallest subunit of the complex, interacts with subunit 10 and ISP, peripherally located
105905 !SQ P07552
81484 ! five transmembrane helices forming a sheet-like structure
81482 ! L and M are probably related to each other
107963 !SQ P02954
107964 !SQ P02953
81443 ! 12 transmembrane helices in an approximate threefold rotational symmetric arrangement
81441 ! the largest and best conserved subunit, contains two heme groups, low spin heme a and high spin heme a3
81453 ! core: 7 transmembrane helices organized into two bundles, one formed by the first two helices and the other by the rest
81451 ! function unknown, possibly involved in the assembly or form the entrance to "oxygen" channel
81334 ! two antiparallel transmembrane helices
81459 ! the "missing" first helix is complemented by the ba3 subunit IIa
71237 ! Ala20Pro/Pro64Ala substituted
73629 ! Ala24/Asp61 to Asp24/Asn61 substituted
81337 ! core: up-and-down bundle of four transmembrane helices
81339 ! core: 8 helices, 2 short helices are surrounded by 6 long transmembrane helices
56895 ! duplication: consist of two similar structural parts
98955 ! single-crystal electron diffraction structure
56898 ! glycerol conducting channel, related to aquaporin
111351 ! 11 transmembrane helices; duplication: consist of 2 structural repeats of five helices each plus extra C-terminal helix
107723 !SQ P37905 2-407
107719 !SQ P37905 2-407
107711 !SQ P37905 2-407
103472 ! 12 transmembrane helices; duplication: the N- and C-terminal halves are structurally similar 
81341 ! core: 18 transmembrane helices
69912 ! duplication: consist of two similar structural parts
81325 ! oligomeric transmembrane alpha-helical proteins
68130 ! residues 22-124
105271 !SQ Q54397 22-124
68135 ! residues 22-124
67354 ! complexed with TBA (tetrabutylammonium) and rubidium
62752 ! residues 24-121
43655 ! residues 1-125
67078 ! open gate model, residues 86-119; CA-atoms only
43659 ! full-length fold; CA-atoms only
67074 ! open gate model, residues 86-119; CA-atoms only
75643 ! calcium gated potassium channel
87353 ! perimeter subdomain only
87348 ! gate and perimeter subdomains
81328 ! oligomeric transmembrane alpha-helical protein
60251 ! gating domain in complex with calmodulin
68668 ! solution free structure
81331 ! oligomeric transmembrane alpha-helical protein
56904 ! Large-conductance ion channel
90111 ! heteropentameric transmembrane alpha-helical protein; 4 transmembrane helices per subunit
82860 ! oligomeric fold; 3 transmembrane helices per subunit
82863 ! homoheptameric protein
103480 ! oligomeric fold; 3 transmembrane helices per subunit
103485 ! 9 transmembrane helices
103486 ! duplication: consists of three similar structural parts 
103490 ! 10 transmembrane helices forming of a gated channel
103491 ! duplication: consists of two similar structural parts 
81559 ! core:11 transmembrane helices
81557 ! Photosystem I p700 chlorophyll a apoprotein a1/a2
81564 ! core: hairpin of two transmembrane helices
81569 ! core: three transmembrane helices, bundle
81346 ! multihelical; complex architecture with several transmembrane helices
90122 ! multihelical; complex architecture with several transmembrane helices
90125 ! a low-resolution structure of the E.coli MsbA in an open conformation is also available </i>(<a href="../search.cgi?sccs=f.35.1.1">f.35.1.1</a>)<i>
88059 ! structure in a closed conformation
82865 ! 12 transmembrane helices; duplication: the N- and C-terminal halves of the whole proteins are structurally similar
81649 ! core: three transmembrane helices, up-and-down bundle
81647 ! a part (domain) of mitochondrial cytochrome b subunit, separate subunit in plants and cyanobacteria
104271 !SQ P00157
104241 !SQ P00157
105894 !SQ P00157
81344 ! core: four transmembrane helices, up-and-down bundle, binds one or two heme groups in between the helices
81342 ! Three of the four heme-ligands are conserved between the two families; both heme groups bind similarly but not identically
81642 ! a part (domain) of a larger mitochondrial cytochrome b subunit, separate subunit in plants and cyanobacteria
81641 ! also includes extra transmembrane (linker) helix absent in plants and cyanobacteria subunits
104272 !SQ P00157
104242 !SQ P00157
105895 !SQ P00157
103501 ! possible link between the two other superfamilies: this subunit corresponds to the gamma subunit of a functionally related Formate dehydrogenase N complex but is structurally closer to the Fumarate reductase subunit FrdC
105592 !SQ P11350
81343 ! two distinct families: in one family the common fold is contained in a single-chain subunit, in the other it is formed by two chains
56910 ! duplication: consists of two structural repeats; the heme-binding sites are related by pseudo two fold symmetry
81373 ! consists of two homologous non-identical subunits that form a heterodimer; may or may not contain heme groups
82870 ! Cytochrome b556 subunit
82872 ! membrane anchor protein
81369 ! is not known to bind heme
81371 ! is not known to bind heme
81525 ! membrane-associated alpha-helical protein; no transmembrane helices
81524 ! location - matrix side of the bc1 complex
81523 ! probably important for the complex assembly, caps the matrix face of cytochrome b
104277 !SQ P00129
104247 !SQ P00129
105900 !SQ P00129
81532 ! membrane-associated alpha-helical protein; no transmembrane helices
81531 ! location - intermembrane side of the bc1 complex
81530 ! "acidic/hinge protein", essential for the complex formation, interacts with the functional domain of cytochrome c1
104279 !SQ P00126
104249 !SQ P00126
105902 !SQ P00126
111356 ! 2 helices, hairpin
108972 !SQ P02721 33-108
81666 ! core: multihelical; consists of three transmembrane regions of 2, 2 and 6 helices, separated by cytoplasmic domains
81663 ! the N-terminal 40 residues interact with /form a part of transduction domain A
106476 !SQ P04191
108583 !SQ P04191
106480 !SQ P04191
75861 ! Structure in the absence of calcium ions
75895 ! Structure in the e2 state
56917 ! membrane all-alpha fold
66988 ! structure in detergent micelles
103505 ! membrane all-alpha fold; 6-helical "barrel" with internal binding cavity
103506 ! duplication: consists of three alpha-hairpin repeats
103510 ! membrane all-alpha fold; three transmembrane helices
103511 ! duplication: contains two structural repeats
103513 ! part of chloroplast major light-harvesting complex; see also low-resolution structure of pea protein, PDB entry 1VCR
56924 ! not a true fold, gathers together transmembrane barrels of different (n,S)
56925 ! forms (8,10) barrel
104589 !SQ P36546
106920 !SQ Q7C2L2
69917 ! forms (10,12) barrel
103515 ! forms (12,14) barrel; contains a long alpha-helix running along the barrel axis
56931 ! forms (12,16) barrel
56936 ! trimer, one subunit folds into (16,20) barrel
76703 ! engineered asymmetric conductivity
43771 ! osmoporin ompk36
64534 ! Anion-selective porin OMP32
59258 ! complexed with a periplasmic peptide, chain B
56942 ! trimer, one subunit folds into (18,22) barrel
56948 ! monomeric (22,24) barrel; ~150 N-terminal residues form a "plug" or "cork" subdomain
43804 ! complex with bound ferrichrome-iron
59844 ! complex with lipopolysaccharide
90129 ! vitamin B12 receptor
99471 ! complexed with colicin e3 receptor binding domain
111361 ! monomeric (14,16) barrel; plugged by an N-terminal all-alpha subdomain (1-40)
106243 !SQ P10384
106253 !SQ P10384
111364 ! forms (12,16) barrel 
107144 !SQ P22786
107142 !SQ P22786
107146 !SQ P22786
56953 ! subunit fold contains tandem repeat of alpha-beta hairpin-alpha(2) motif ! trimeric fold contains barrel (n=12, S=18) formed by beta-hairpins, two from each subunit, and a bundle of helices with a channel running through it
107244 !SQ P02930
111368 ! consists of three domains: beta-barrel (res. 29-38,170-259; scop_cf 50412); barrel-sandwich hybrid (39-72,135-169; scop_sf 51230) and long alpha-hairpin (73-134; scop_cf 46556)
108569 !SQ P52477 #! periplasmic component of efflux pump; channel-forming oligomer, interacts with TolC
106448 !SQ P52477 #! periplasmic component of efflux pump; channel-forming oligomer, interacts with TolC
56958 ! subunit fold contains beta-sandwich of Ig-like (grerk-key) topology and a beta-ribbon arm that forms an oligomeric transmembrane barrel
56960 ! heptameric fold contains barrel (n=14, S=14) formed by beta-ribbon arms, one from each subunit
106472 !SQ O80066
103519 ! octameric fold contains barrel (n=16, S=16) formed by beta-ribbon arms, one from each subunit
56967 ! contains several large open beta-sheets
56972 ! 3 domains: (1) alpha+beta; (2&3) all-beta
56975 ! contains the APT module at the N-terminus
108145 !SQ Q57398
56977 ! 2 domains: (1) alpha+beta; (2) all-beta, similar to the CalB domain fold but the two last strands are transposed
56982 ! 2 intertwined domains; all-beta and alpha+beta
106893 !SQ P12823 281-675 # 99% sequence identity
106915 !SQ P12823 281-675 # 99% sequence identity
106899 !SQ P12823 281-675 # 99% sequence identity
111378 ! 2 domains; d1: complexed all-beta fold; d2: coiled-coil (trimeric) helical region
105724 !SQ Q91HI9 253-522
69921 ! 3 intertwined all-beta domains
111383 ! trimer; one subunit consists of an alpha/beta oligomerization subdomain [3-stranded parallel beta-sheet, order 213], and an antiparallel coiled coil
107614 !SQ P11457
105521 !SQ P11457
56987 ! 4 domains; I (res. 14-225) and II (226-487) are beta-sandwiches of similar gamma-crystallin like topologies; III (488-594) has a beta-grasp like fold; IV (595-735) has an Ig-like fold
106556 !SQ P13423
107519 !SQ P13423
56993 ! nearly all-alpha ! can be classified as disulfide-rich
43950 ! single chain insulin analog mutant
70583 ! structure at pH 2: the conditions promoting insulin fibre formation
62671 ! an unstable insulin analog with native activity
62875 ! an unstable insulin analog with enhanced(?) activity
43891 ! an active mini-proinsulin, m2pi
43942 ! superpotent single-replacement insulin analogue
98827 ! solution structure under amyloidogenic condition
66503 ! a monomeric mutant (PT insulin) ! Alpha-galactosidase agl1
106261 !SQ P01308
106260 !SQ P01308
106251 !SQ P01308
43968 ! cross-linked b28 asp single-chain design
70880 ! complex with IGFBP-5
94917 ! bound to a phage-derived peptide, chain B
43991 ! C-region deleted
57006 ! disulfide crosslinked alpha-helical hairpin
57008 ! contains 2 disulfides
57012 ! contains 4 disulfides
111388 ! contains 3 disulfides
105975 !SQ O24172
57015 ! disulfide-bound fold; contains beta-hairpin with two adjacent disulfides
57018 ! one subunit consists of four homologous domains
57020 ! consists of two homologous domains
57022 ! single domain
106234 !SQ P02877 18-49
103522 ! consists of three homologous domains
103524 ! consists of two homologous domains
99396 ! isoform D2
99570 ! isoform D1
99568 ! isoform D2
104091 !SQ P83597
104096 !SQ P83597
103811 !SQ P12071
103813 !SQ P12071
78951 ! hybrid inhibitor HEI-TOE containing the grafted loop from the ovomucoid 3rd domain
57038 ! macrocyclic plant knottins closed with the formation of an Asn-Gly peptide
57040 ! cyclic 29-residue polypeptide
79823 ! in the linear precursor, the mature protein sequence begins at Gly 26 and ends at Asn 25
104306 !SQ P58454 71-97
85507 ! in the precursor, the mature protein sequence begins at Gly26 and ends at Asn25
71699 ! in the linear precursor, the mature protein sequence begins at Gly 9 and ends at Asn 8
44077 ! in the linear precursor, the mature protein sequence begins at Gly 9 and ends at Asn 8
72052 ! in the linear precursor, the mature protein sequence begins at Gly 9 and ends at Asn 8
87370 ! acyclic permutant; canonical knottin topology
57043 ! cyclic 30-residue polypeptide
85524 ! by homology with Kalata, in the precursor, the mature protein sequence probably begins at Gly28 and ends at Asn27
44078 ! by homology with the Kalata B1 linear precursor, the mature protein sequence probably begins at Gly25 and ends at Asn24
57046 ! cyclic 30-residue polypeptide
44079 ! by homology with the Kalata B1 linear precursor, the mature protein sequence probably begins at Gly28 and ends at Asn27
96815 ! by homology with the Kalata B1 linear precursor, the mature protein sequence probably begins at Gly35 and ends at Asn34
107304 !SQ P01522 46-72
107286 !SQ P01522 46-72
107303 !SQ P05484 46-70
107288 !SQ P05484 46-70
82878 ! Spasmodic conotoxin
105014 !SQ Q26443
44110 ! Hairpinless mutant
76722 ! C-terminal truncation (ct-hv2a)
107462 !SQ Q7YT39 47-80
57093 ! scorpion toxin with a spider toxin-like fold
90132 ! scorpion toxin with a spider toxin-like fold
90135 ! a plant hormone
103537 ! insecticidal protein
105453 !SQ P01484 ! Aah2: chimeric toxin
106624 !SQ P45697
106620 !SQ P45697
106621 !SQ P45697
80685 ! atomic resolution structure
104122 !SQ P63019
57111 ! Anti-mammal and anti-insect scorpion toxin
44154 ! two disulfide derivative
44153 ! curaremimetic chimeric protein
44166 ! misfolded?
57158 ! nontoxic peptide?
104381 !SQ Q86QT3 21-62
104333 !SQ Q95NK7
109406 !SQ Q9U8D2
109407 !SQ Q9U8D1
65987 ! antifungal protein
65988 ! an antifungal and antibacterial mutant
57164 ! inducible antifungal protein
103556 ! flower-specific gamma-thionin
57178 ! sweet protein
70881 ! complex with IGF
57188 ! contains 3 cystine-knot subdomains and 4 single-disulfide cystine knot-like subdomains
91379 ! complexed with TGF-alpha
86036 ! complexed with EGF
76852 ! complexed with EGF
57192 ! duplication: consists of two (sub)domains of this common fold
77436 ! C-terminal domain
103882 !SQ P08709 107-202
77438 ! C-terminal domain
103843 !SQ P08709 108-202
44223 ! N-terminal domain
44221 ! N-terminal domain
44224 ! N-terminal domain
44220 ! N-terminal domain
44222 ! N-terminal domain
57210 ! the rest of protein is heme-linked peroxidase, all-alpha fold
107698 !SQ P05979 32-584
70209 ! EGF/TGFalpha chimera
86037 ! complexed with EGF receptor
76854 ! complexed with EGF receptor
94391 ! EGF/TGFalpha chimera
91381 ! complexed with EGF receptor
57219 ! extracellular domain
57227 ! duplication: contains 47 EFG-like domains
100233 ! CBEGF22 and CBEGF23
100230 ! CBEGF22 and CBEGF23
100236 ! CBEGF22 and CBEGF23
44321 ! 39th and 40th calcium-binding EGF-like domains
84632 ! 12th and 13th calcium-binding EGF-like domains
44323 ! 39th and 40th calcium-binding EGF-like domains
90141 ! EGF-like domain separates two CUB domains
106148 !SQ O00187 17-181
80239 ! modules A, B, and C in the whole receptor structure context
73558 ! EGF-like module 3
60623 ! partly disordered
57237 ! the N-terminal part of FS module
90145 ! the N-terminal part of the heparin-binding module, FS1
57245 ! duplication: consists of two subdomains of this fold
44339 ! uncertain order of chains in precursor protein
44341 ! uncertain order of chains in precursor protein
57249 ! duplication: consists of two sequence repeats each having this fold
57254 ! further duplication: consist of two BBI domains
44351 ! partly disordered
57268 ! duplication: consists of two similar domain
44369 ! CA-atoms only
61398 ! C-terminal domain
57282 ! disulfide-rich fold; all-beta: 3 antiparallel strands
109439 !SQ Q8WQ22 23-57 # Locusta migratoria migratorioides
57287 ! disulfide-rich fold; all-beta: 3 antiparallel strands
82894 ! disulfide-rich fold; all-beta: 3 antiparallel strands
78179 ! repeats 2 and 3 (res. 434-546)
57295 ! disulfide-rich; alpha+beta: 3 antiparallel strands followed by a short alpha helix
57301 ! disulfide-rich fold: nearly all-beta
57308 ! different isoforms
44405 ! engineered chimera with alpha-toxin
90152 ! acetylcholine receptor binding protein
82899 ! identical sequence to the <i>Naja naja siamensis</i> toxin
78294 ! complexed to a cognate peptide, chain B
78295 ! complexed to a cognate peptide, chain B
65787 ! complexed with high affinity peptide
60878 ! complexed with a high affinity 13-mer peptide
44429 ! complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
73947 ! complexed with an ACHR peptide, chain B
60877 ! complexed with a high affinity 13-mer peptide
62526 ! complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
62844 ! complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
72293 ! complex with the principal binding sequence on the alpha7 subunit of a neuronal nicotinic acetylcholine receptor, chain B
62297 ! complexed to an 18mer cognate peptide
73570 ! complexed with an ACHR peptide, chain B
72680 ! complex with the principal binding sequence on the alpha7 subunit of a neuronal nicotinic acetylcholine receptor, chain B
62296 ! complexed to an 18mer cognate peptide
97439 ! complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
103847 !SQ Q9YGJ0 22-89
44441 ! solution structure in dpc-micelle
108899 !SQ P83346
57352 ! lacks neurotoxicity; acts as the disintegrins: contains RGD-motif
44458 ! CA-atoms only
84733 ! complexed with BMP7
86415 ! complexed with activin A
86427 ! complexed with activin A
105258 !SQ P27040 23-120 # ! Structural genomics target; 100% sequence identity to the rat domain of the same type IIb (scop_sp 90154)
69951 ! elaborated with additional structures resulting in a beta-sandwich fold
68868 ! complex with tgf-beta3
57361 ! disulfide-rich alpha+beta fold
60320 ! Ultra high resolution structure; 0.86 Angstrom
68233 ! a cyclic variant
44506 ! dodecamer observed in the crystals
44532 ! dodecamer observed in the crystals
44541 ! second kunitz domain
44542 ! second kunitz domain
66288 ! third kunitz domain
57387 ! duplication: consists of two BPTI-like domains
57391 ! Disulfide-rich fold, nearly all-beta
90157 ! structurally similar to beta-defensin
57413 ! alpha+beta fold with two crossing loops
57414 ! the middle part is structurally similar to some knottins and defensins but differs in the disulfide pattern
57416 ! heparin-binding domain
82901 ! probable carbohydrate-binding function
57418 ! disulfide-rich fold
57423 ! disulfide-rich calcium-binding fold
44609 ! fifth module
66437 ! seventh module
44615 ! first module
44612 ! sixth module
44611 ! a concatemer of the first and second modules
44616 ! second module
44614 ! complement-like repeat cr3
44613 ! complement module 8
44617 ! sixth module
80245 ! all but the first modules in the whole receptor structure context
69953 ! the viral-binding domain of Tva
100553 ! LDL-receptor class A domain 3
57428 ! disulfide-rich alpha+beta fold
44618 ! ultra-high resolution
57439 ! disulfide-rich fold; nearly all-beta
44629 ! kringle 4
44630 ! kringle 4
44643 ! kringle 5
44645 ! kringle 1
72495 ! Angiostatin: the N-terminal fragment containing three kringles
44634 ! kringle 4
44631 ! kringle 4
44639 ! kringle 2
44648 ! kringle 1
44646 ! kringle 1
44636 ! kringle 4
61790 ! kringle 2; complexed to an internal peptide from a group A streptococcal surface protein
44641 ! kringle 2
44640 ! kringle 2
44649 ! kringle 1
44650 ! kringle 1
57459 ! shorter two-disulfide version of a kringle module
57464 ! duplication: tandem repeat of three modules inserted in the catalytic domain
44677 ! second module only
62699 ! third module only
68856 ! first module only
75674 ! duplication: tandem repeat of three modules inserted in the catalytic domain
100895 ! conserved core consists of a helix and a loop crosslinked with two disulfides
57469 ! unless specified in the comment, the listed structures are of domain III
96740 ! second domain 
57476 ! duplication: contains two domains of this fold
72743 ! Domain I only
57478 ! the C-terminal part of FS module
90166 ! the C-terminal part of the heparin-binding module, FS1
69961 ! kazal-type 5 serine protease inhibitor; consists of several similar domains
65808 ! domain 1
83445 ! domain 6
108045 !SQ Q9NQ38 28-77  ! chimeric lekti-domain
100896 ! disulfide-rich small alpha+beta fold; topological similarity to the Ovomucoid domain III
44725 ! T1 domain
44728 ! single sequence repeat
44729 ! C2 domain
44727 ! C1-T1 two-domain derivative of the circular precursor protein Na-ProPI
90168 ! two-domain inhibitor; consists of one continuous domain of canonical fold and one discontinuous, circularly-permutated domain
57491 ! disulfide-rich fold; common core is alpha+beta with two conserved disulfides 
57494 ! duplication: consists of two homologous domains
44741 ! CA-atoms only
57496 ! single trefoil motif protein
103576 ! Pfam 01437
105566 !SQ P08581 40-564
103579 ! disulfide-rich fold; all-beta; duplication: contains two structural repeats 
57500 ! disulfide-rich fold; common core is all-beta
107486 !SQ P15692 40-133
107491 !SQ P15692 40-133
77310 ! complexed with a phage-derived peptide antagonist, chains X and Y
79241 ! disulfide deficient mutant
79215 ! disulfide deficient mutant
79237 ! disulfide deficient mutant
68867 ! complexed with the type II receptor extracellular domain
84732 ! complexed with the extracellular domain of activin type II receptor
105259 !SQ P08476 311-426 # ! Structural genomics target
86416 ! complexed with the extracellular domain of activin type II receptor
86428 ! complexed with the extracellular domain of activin type II receptor
82905 ! BMP-7 antagonist
44793 ! heterodimer with NT3
44797 ! heterodimer with NT4
44794 ! heterodimer with BDNF
44798 ! heterodimer with BDNF
65789 ! homodimer
44800 ! homodimer
105514 !SQ P01138
57534 ! disulfide-rich all-beta fold
44819 ! 15th module only
44820 ! 16th module only
44822 ! both modules
57540 ! a complement protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans
104950 !SQ P10998 
44844 ! central cp module pair
44862 ! N-terminal two domains
57543 ! consists of five modules with the C-terminal module fold being altered
44873 ! fifth module
44874 ! fifth module
83414 ! modules 3 and 4
83416 ! modules 3 and 4
93215 ! intact protein 
93155 ! intact protein 
93199 ! intact protein 
93207 ! intact protein 
93163 ! intact protein 
93189 ! intact protein 
99705 ! modules 3 and 4
83467 ! modules 3 and 4
90549 ! modules 3 and 4
93245 ! intact protein 
86305 ! modules 2 and 3; a functionally active component of Daf
99765 ! modules 3 and 4
94980 ! module 16
70230 ! modules 15 and 16
70220 ! modules 16 and 17
60525 ! complexed with C3D
104529 !SQ O00187 366-686
57545 ! disulfide-rich all-alpha fold
57551 ! small disulfide-rich
79998 ! refined solution structure
104552 !SQ P30403 408-475
104551 !SQ P30403 408-475
82908 ! non-RGD disintegrin; conserved cysteines form different disulfides (?)
106816 !SQ P83658 # sequence identity to chain A: 87%, to B: 85%
105018 !SQ P83658
57560 ! disulfide-rich; nearly all-beta
57566 ! disulfide-rich; nearly all-beta
57580 ! disulfide-rich; alpha+beta
57582 ! transforming growth factor beta binding protein-like domain
100234 ! TB4
100231 ! TB4
100237 ! TB4
91026 ! third TB domain
57585 ! duplication: consists of three similar disulfide-rich domains
57587 ! TNFR/NGFR cysteine-rich region (Pfam 00020)
105518 !SQ P07174 31-190 # fragment contains 3 complete and 1 partial (c-terminal) 'domains'
90174 ! only fragments of the receptor structures are available; no domain division is provided here
90176 ! also includes the PDB entry </i>(<a href="../pdb.cgi?pdb=1p0t">1p0t</a>)<i> that together with the entry </i>(<a href="../pdb.cgi?pdb=1otz">1otz</a>)<i> provides the multimeric structure of the complex of BAFF receptor with BAFF. In these entries protein chains are designated by both upper case and lower case letters creating problems with its processing and presentation in SCOP
57592 ! duplication: consists of two similar disulfide-rich domains, alpha+beta
57597 ! disulfide-rich; all-beta: open barrel, 5 strands; OB-fold-like
57602 ! disulfide-rich, all-beta
86687 ! 1st and 2nd modules in complex with a peptide from the streptococcal fibronectin binding protein, FnbB, chain B
44949 ! 4th & 5th modules
44954 ! part of the gelatin-binding domain
44950 ! part of the gelatin-binding domain
44951 ! part of the gelatin-binding domain
44953 ! 1st and 2nd modules
57609 ! disulfide-rich, alpha+beta
57611 ! Pfam 00086
105013 !SQ P24592 161-240
57614 ! disulfide-rich, alpha+beta
64570 ! disulfide-rich, alpha+beta
57619 ! disulfide-rich, alpha+beta
57624 ! disulfide-rich
57625 ! shares a putative chitin-binding motif with the plant lectins/antimicrobial peptides superfamily but lacks one of the conserved disulfides of the knottin fold
57627 ! an antimicrobial protein with chitin-binding function
69963 ! disulfide-rich, all-alpha
90182 ! disulfide-rich; all-alpha
82909 ! disulfide-rich, alpha+beta
90187 ! disulfide-rich
105998 !SQ P04004 20-70
105253 !SQ P04004 20-70
90192 ! disulfide-rich; all-alpha; calcium-binding
90194 ! also called DSL domain or LNR repeat
103588 ! disulfide-rich
105867 !SQ Q00484 126-149
111417 ! disulfide-rich all-beta fold; contains beta sandwich of 5 strands
107634 !SQ Q60748 39-133
111422 ! disulfide-rich six-stranded beta-sandwich; jelly-roll
104934 !SQ Q99P87 26-114 # contains alpha-helical oligomerization subdomain(26-51; trimeric right-handed coiled coil)
104921 !SQ Q99P87 26-114 # contains alpha-helical oligomerization subdomain(26-51; trimeric right-handed coiled coil)
104942 !SQ Q99P86 25-105
111429 ! bipartite cysteine-rich all-alpha domain; a single helix in the N-terminal part (chain A) is linked by disulfides to the C-terminal part (chain B) [3-helical bundle of the RuvA C-terminal domain-like fold (scop_cf 46928) 
105981 !SQ P19880 279-313,565-650
57629 ! Calcium ion-bound
57630 ! gamma-carboxy-glutamic acid-rich domain
57641 ! a few helical turns and a disulfide-crosslinked loop
44976 ! complex with cholecystokinin-8
57646 ! a few helical turns assembled without a hydrophobic core?
57651 ! folds around 4Fe-4S cluster
57661 ! folds around 4Fe-4S cluster
57666 ! alpha+beta metal(zinc)-bound fold: beta-hairpin + alpha-helix
57669 ! duplication: consists of 3 fingers
91062 ! chimera with GCN4 coiled-coil region, C:157-187 and D:257-285
45032 ! C-terminal domain
45033 ! N-terminal domain
45034 ! N-terminal domain
45035 ! N-terminal domain
72722 ! ZFY-6T domain
72723 ! ZFY-6T domain
45037 ! ZFY-6T domain
45038 ! ZFY-swap domain
45039 ! domain 2
45040 ! domain 1; has an extension to the common fold at the N-terminus
57685 ! duplication: consists of two Zn fingers
45049 ! Single zinc finger
45048 ! Single zinc finger
45050 ! finger 2
45051 ! finger 3
57691 ! duplication: consists of 4 fingers
57693 ! duplication: consists of 6 fingers
45059 ! fingers 1-3
94216 ! finger 3
105966 !SQ O35615 328-360
45074 ! the ninth zinc-finger domain
45075 ! the first zinc finger
77139 ! CCHH mutant of the ninth zinc-finger domain
108064 !SQ P09234 1-61
57700 ! all-alpha dimetal(zinc)-bound fold
57701 ! duplication: two structural repeats are related by the pseudo dyad
57715 ! alpha+beta metal(zinc)-bound fold
57717 ! single zinc-binding motif
57721 ! duplication: two zinc-binding motifs
57729 ! identical sequences
104802 !SQ P15207 538-611 # 98% sequence identity
103606 ! protein-protein interaction module
57736 ! duplication: contains two (sub)domains of this fold
86412 ! fourth LIM domain
45148 ! first LIM domain
84021 ! fusion of the first LIM domain with a fragment of LIM domain binding protein 1, LMBP1, residues 75-114, connected with a linker, res. 64-74
84795 ! fusion of the first LIM domain with a fragment of LIM domain binding protein 1, LMBP1, residues 83-122, connected with a linker, res. 72-82
108397 !SQ Q6H8Q1 73-140 # ! Structural genomics target
105340 !SQ P14116
82914 ! Zn-binding site is particularly similar to that of ribosomal protein L24e
96894 ! bound to 5,6-Dihydrouracil (DhU) containing DNA
75913 ! covalent-DNA intermediate
75910 ! bound to abasic-site containing DNA
75922 ! DNA estranged guanine mismatch recognition complex
75919 ! DNA estranged thymine mismatch recognition complex
96891 ! bound to 8-Oxoguanine (OxoG) containing DNA
75916 ! DNA end-product structure
75877 ! covalently trapped with DNA
106789 !SQ P42371
104166 !SQ P42371
104163 !SQ P42371
104192 !SQ P42371
104520 !SQ P50465
104523 !SQ P50465
104517 !SQ P50465
106774 !SQ Q96FI4 1-333
108063 !SQ P49916 1-117
111448 ! Pfam coverage extends to the second helix of the upstream alpha-hairpin domain
107046 !SQ P18274 7-151 
103611 ! consist of two different zn-binding subdomains, each subdomain resembles a distorted glucocorticoid receptor-like fold
103613 ! Pfam 03110
57755 ! metal(zinc)-bound fold
57760 ! duplication: two similar zinc-binding motifs
104531 !SQ P03350 389-429
104530 !SQ P03350 389-429
45172 ! contains a sequence of the psi-packaging domain of HIV-1
57769 ! metal(zinc or iron)-bound fold; sequence contains two CX(n)C motifs, in most cases n = 2
57771 ! in the Pyrococcus abyssi MetRS structure there is a tandem repeat of two such domains swapped with their zinc-binding 'knuckles', this duplicated finger occupies a larger region (124-183) than defined below; there is a structurally equivalent region in the E. coli enzyme lacking the second zinc-binding site
105065 !SQ Q9V011 1-606 # C-domain 616-722 is solved separately: 1MKH
57778 ! contains a rudiment form of the domain that lacks zn-binding site
57779 ! contains a rudiment "zinc-finger" subdomain
57780 ! contains a rudiment "zinc-finger" subdomain
57781 ! contains a rudiment "zinc-finger" subdomain
45203 ! contains a rudiment "zinc-finger" subdomain
105022 !SQ Q00403 2-59
104988 !SQ Q00403 2-59
57787 ! contains two differently decorated domains of this fold
45205 ! C-terminal domain
57792 ! contains alpha-helices in the N- and C-terminal extensions (linkers?)
57795 ! Duplication: contains tandem repeats of several domains with zinc-binding sites being lost in some of them
45211 ! both domains are zinc-less
57799 ! contains alpha-helices in the N- and C-terminal extensions (linkers?)
96728 ! cadmium-substituted
96725 ! gallium-substituted 
96726 ! mercury-substituted
96727 ! cobalt-substituted
96729 ! nickel-substituted 
45241 ! variant pfrd-xc4 folds without iron
45242 ! zn-substituted
108516 !SQ P24297
98366 ! second domain
105231 !SQ P24931
105233 !SQ P24931
92009 ! structural genomics
57814 ! dimeric mono-domain protein with two rubredoxin-type metal centres
45250 ! Ga-substituted
45252 ! complexed with Cd2+
45254 ! Hg-substituted
108970 !SQ Q46495 # 
108966 !SQ Q46495 # 
108962 !SQ Q46495 # 
57818 ! membrane-anchored rubredoxin-like domain
94511 ! complexed with a snare peptide
94501 ! complexed with a snare peptide
94506 ! complexed with a snare peptide
90209 ! contains CxxxxC-x(n)-CxxC zinc-binding site; similar to the Sec23/24 zinc finger domain
103623 ! contains CxxC-x(n)-CxxxxC zinc-binding site; sequence similarity to NAD-dependent DNA ligase zinc-finger subdomain 
95176 ! structural genomics
90214 ! a ubiquitin-interacting domain
57821 ! contains two CXC motifs
57822 ! possible metal-binding fold
107344 !SQ P00478
104714 !SQ P00478
104588 !SQ P00478
107315 !SQ P00478
107302 !SQ P00478
104706 !SQ P00478
104149 !SQ 
105345 !SQ P60619
96527 ! structural genomics; NESG target GR2
105126 !SQ Q8U440 # ! Structural genomics target
57839 ! zinc-bound beta-ribbon motif
75688 ! zinc-bound beta-ribbon motif
57844 ! zinc-bound alpha+beta motif
57849 ! dimetal(zinc)-bound alpha+beta motif; structurally diverse
45322 ! include dimerization helices
66880 ! heterodimer with bard1 RING domain
66881 ! heterodimer with brca1 RING domain
90220 ! binding domain for E2 ubiquitin ligase
108422 !SQ Q8R3P2 389-489 # ! Structural genomics target ! C-terminal RING domain; one zinc ion-bound structure adopts a different fold; misfolded conformation (?)
109232 !SQ Q9Y4X5 336-394
90222 ! Associated with multi-ubiquitination; lacks the RING-domain metal ion-binding residues
111461 ! Armadillo repeat containing protein
106247 !SQ Q8VZ40 249-321
57862 ! zinc-bound alpha+beta motif
57865 ! core is similar to that of the RING finger but lacks one zinc-binding site
57867 ! metal(iron)-bound fold ! duplication: consists of clear structural/sequence repeats
45331 ! Two domains (1-32;33-61)
45334 ! alpha domain
66734 ! alpha domain of metallothionein-3
45335 ! beta domain
84744 ! beta domain
84743 ! alpha domain
71566 ! beta_C domain
71567 ! beta_N domain
45343 ! Ag-substituted
45342 ! Ag-substituted
45345 ! alpha domain
45346 ! beta domain
57878 ! metal(zinc)-bound alpha+beta fold
57883 ! metal(zinc)-bound alpha+beta fold
57886 ! (crystal structure of the rest of protein is also published)
90473 ! refined solution structure
57888 ! dimetal(zinc)-bound alpha+beta fold
97191 ! C1 domain
108380 !SQ list: O80763 Q8LB68; 476-553 # ! Structural genomics target
57902 ! dimetal(zinc)-bound alpha+beta fold
61406 ! complexed with inositol 1,3-bisphosphate
57907 ! protein involved in membrane trafficking and signal transduction
57909 ! contains additional N-terminal long alpha-helix
90226 ! chromodomain-helicase-DNA-binding protein 4
85015 ! second PHD domain
85016 ! second PHD domain with the C-terminal loop replaced by the corresponding loop from WSTF
57916 ! metal(zinc)-bound alpha+beta fold
57917 ! duplication: contains two Zn-binding domains of similar fold
57919 ! Single-stranded DNA-binding protein
57921 ! Single-stranded DNA-binding protein
57923 ! metal(zinc)-bound alpha+beta fold
57926 ! baculoviral inhibitor of apoptosis
45376 ! BIR3 domain complexed to smac
86293 ! BIR3 domain complexed to caspase 9
61606 ! BIR2 domain complexed to caspase 3
45377 ! BIR2 domain
45378 ! BIR3 domain complexed to a 9 residue peptide from smac/diablo
106858 !SQ P98170 241-356
59748 ! BIR3 domain
98814 ! BIR1 complexed with a grim peptide
98813 ! BIR1 complexed with a reaper peptide
66544 ! BIR2 complexed with grim peptide
95822 ! BIR2 complexed with dronc peptide
66545 ! BIR2 complexed with hid peptide
57930 ! contains a long alpha-helix after the common fold
93708 ! complexed with a peptide antagonist, chain F
93713 ! complexed with a peptide antagonist, chain F
93725 ! complexed with a peptide antagonist, chain F
90228 ! metal(zinc)-bound alpha+beta fold
90230 ! C-x8-C-x5-C-x3-H type and similar
90233 ! Zn-binding, all-alpha fold
90234 ! some sequence similarity to the TAZ domain Zn-binding sites
57932 ! all-alpha fold; Zn-binding sites are in the loops connecting helices
45383 ! TAZ2 domain (also CH3 domain)
73685 ! TAZ1 domain; complexed with the C-terminal activation domain (CTAD) of human HIF-1alpha (chain B)
87778 ! CH1 (TAZ1) domain; complexed with Cited2 transactivation domain (chain A)
97250 ! CH1 (TAZ1) domain; complexed with Cited2 transactivation domain (chain A)
73536 ! CH1 (TAZ1) domain; complexed with the C-terminal activation domain (CTAD) of human HIF-1alpha (chain A)
82926 ! alpha-helical fold with two Zn-binding sites
57937 ! metal(zinc)-bound extended beta-hairpin fold
103636 ! metal(zinc)-bound fold
103641 ! metal(zinc)-bound fold
93818 ! complexed with SecB
106077 !SQ P10408 878-899
106076 !SQ P10408 878-899
103646 ! metal(calcium)-bound fold
100146 ! repeats from 4 to 7
57943 ! this is not a true fold; includes oligomers of shorter identical helices
73390 ! complexed with a TANK peptide, chain B
45472 ! complexed with a fragment from B-cell surface antigen CD40
73388 ! complexed with a TANK peptide, chain B
104916 !SQ Q13114 377-568
45478 ! trimeric mutant
97273 ! trimeric mutant
62476 ! trimeric mutant
62470 ! trimeric mutant
97270 ! trimeric mutant
62479 ! trimeric mutant
97276 ! trimeric mutant
45486 ! helix capping mutant
68464 ! designed mutant
62473 ! trimeric mutant
45489 ! trimeric mutant
45493 ! tetrameric mutant
45496 ! trimeric mutant
68476 ! designed mutant
68470 ! designed mutant
45502 ! HIV-1 gp41 trimer-based mutant
97267 ! trimeric mutant
45505 ! trimeric mutant complexed with benzene
109189 !SQ P03069 249-281
109185 !SQ P03069 249-281
109181 !SQ P03069 249-281
109191 !SQ P03069 249-281
109177 !SQ P03069 249-281
109179 !SQ P03069 249-281
60929 ! longer, broken coiled coil
45536 ! heterodimer with C-jun
84182 ! homodimer
45539 ! heterodimer with C-fos
45541 ! homodimer
45548 ! heterodimer with C/ebp beta
45549 ! heterodimer with Atf4
90524 ! homodimer
61077 ! homodimer
104160 !SQ P03621
72882 ! fragment fused with the yeast GCN4 leucine zipper
79497 ! a peptide model of the C-terminus of a striated alpha tropomyosin
58004 ! trimeric coiled-coil domain
58008 ! pentameric coiled-coil
79691 ! complex with vitamin D3
45589 ! complex with all-trans retinol
58011 ! in the central region two triple coiled-coils are stacked end-to-end and interlock with N-terminal tails
45593 ! coiled-coil region only
104896 !SQ P02671 150-209
97353 ! coiled-coil region only
45599 ! coiled-coil region only
78203 ! coiled-coil region only
104906 !SQ P02671 150-209
78193 ! coiled-coil region only
97343 ! coiled-coil region only
45611 ! coiled-coil region only
45617 ! coiled-coil region only
80282 ! coiled-coil region only
45623 ! coiled-coil region only
96424 ! central region only
80292 ! coiled-coil region only
67443 ! central region only (e5 fragment)
67449 ! central region only (e5 fragment)
74324 ! coiled-coil region only
80219 ! coiled-coil region only
45594 ! coiled-coil region only
104898 !SQ P02675
97355 ! coiled-coil region only
45600 ! coiled-coil region only
78205 ! coiled-coil region only
104908 !SQ P02675
78195 ! coiled-coil region only
97345 ! coiled-coil region only
45612 ! coiled-coil region only
45618 ! coiled-coil region only
80284 ! coiled-coil region only
45624 ! coiled-coil region only
96425 ! central region only
80294 ! coiled-coil region only
67444 ! central region only (e5 fragment)
67450 ! central region only (e5 fragment)
74326 ! coiled-coil region only
80221 ! coiled-coil region only
45595 ! coiled-coil region only
104900 !SQ P02679
97357 ! coiled-coil region only
45601 ! coiled-coil region only
78207 ! coiled-coil region only
104910 !SQ P02679
78197 ! coiled-coil region only
97347 ! coiled-coil region only
45613 ! coiled-coil region only
45619 ! coiled-coil region only
80286 ! coiled-coil region only
45625 ! coiled-coil region only
96426 ! central region only
80296 ! coiled-coil region only
67445 ! central region only (e5 fragment)
67451 ! central region only (e5 fragment)
74328 ! coiled-coil region only
80223 ! coiled-coil region only
94390 ! cortexillin I/GCN4 hybrid peptide
66179 ! complexed with a DNA ligase IV peptide
45631 ! CASP4
70212 ! coil 1A fragment ! coil 2B fragment linked to GCN4 leucine zipper
70211 ! coil 2B fragment linked to GCN4 leucine zipper
70208 ! coil 2B fragment
58030 ! not a true superfamily
73927 ! complexed with eIF4G peptide, chains C and D
58038 ! tetrameric parallel coiled coil
80271 ! complex with syntaxin and SNAP-25 fragments
72518 ! complex with SNAP25, syntaxin and complexin fragments
45651 ! complex with syntaxin and SNAP-25 fragments
73559 ! complex with SNAP25, syntaxin and synaphin fragments
65278 ! complex with syntaxin 7, VTI1B and syntaxin 8
88909 ! a globular structure of a larger fragment containing this region is available; </i>(<a href="../pdb.cgi?pdb=1dn1">1dn1</a>)<i>, chain B
80272 ! complex with synaptobrevin and SNAP-25 fragments
107995 !SQ P32851 196-259
67273 ! complex with SNAP25 fragments
45642 ! Self-association H3 region of syntaxin 1A
72519 ! complex with SNAP25, synaptobrevin and complexin fragments
45652 ! complex with synaptobrevin and SNAP-25 fragments
73560 ! complex with SNAP25, synaptobrevin and synaphin fragments
88911 ! complex with endobrevin, VTI1B and syntaxin 8
65281 ! complex with endobrevin, VTI1B and syntaxin 7
85722 ! N-terminal region (homotetramer)
88915 ! provides up to two different helical regions to synaptic fusion complexes
88916 ! identical sequences to human species
80274 ! complex with synaptobrevin and syntaxin fragments
107997 !SQ P13795 7-83; 142-204 # separate coverage for chains C and D
67272 ! complex with syntaxin fragments
45654 ! complex with synaptobrevin and syntaxin fragments
88917 ! identical sequences to rat species
72521 ! complex with syntaxin, synaptobrevin and complexin fragments
73562 ! complex with syntaxin, synaptobrevin and synaphin fragments
65280 ! complex with endobrevin, syntaxin 7 and syntaxin 8
72522 ! complex with SNAP25, synaptobrevin and syntaxin fragments
73563 ! complex with SNAP25, synaptobrevin and syntaxin fragments
107994 !SQ Q9Z152
58044 ! forms trimer
58048 ! biological unit: trimer; fragmented coiled coil capped with beta-hairpin triplet
108254 !SQ P10104 
108260 !SQ P10104 
97395 ! beta-hairpin triplet (foldon) only; no coiled-coil structure
93668 ! mini-fibritin mutant ! beta-hairpin triplet (foldon) only; no coiled-coil structure
45658 ! deletion mutant M
58056 ! a naturally occurring parallel right-handed coiled-coil tetramer
104187 !SQ P11978 1272-1346
90250 ! form heterodimeric coiled coil
85828 ! contains a fragment of the yeast GCN4 leucine zipper
106566 !SQ O75496 110-145
107865 !SQ O75496 70-152
109402 !SQ O88513 79-156 # chains B and E coverage
58059 ! tetrameric antiparallel bundle with a right-handed twist
58063 ! core: trimeric coiled coil
58066 ! trimer
97948 ! 1934 human H1
97900 ! 1930 swine H1
97936 ! 1930 swine H1
45679 ! low pH conformer
97888 ! 1930 swine H1
97960 ! 1934 human H1
97848 ! 1934 human H1
97313 ! 1918 human H1
97894 ! 1918 human H1
58071 ! coiled coil; biological unit: trimer
45720 ! fusion protein between gp41 and GCN4 fragments; complex with a d-peptide inhibitor of HIV-1 entry
76423 ! fusion protein between gp41 and GCN4 fragments; complex with a cell entry inhibitor
45728 ! fusion protein between gp41 and GCN4 fragments; complex with a cell entry inhibitor
45731 ! ectodomain
45752 ! ectodomain
45743 ! ectodomain
45740 ! ectodomain
45749 ! ectodomain
45746 ! ectodomain
45737 ! ectodomain
45753 ! chimera with MBP
45762 ! chimeric, contains a fragment of gcn4 zipper at the N-terminus (res. 1-29)
58078 ! trimer of heterodimers
109249 !SQ P11224 969-1024,1224-1254 # 1WDF (970-1024); 1WDG (969-1008,1224-1254)
109247 !SQ P11224 969-1024,1224-1254 # 1WDF (970-1024); 1WDG (969-1008,1224-1254)
109433 !SQ P59594 902-948, 1144-1176 
58086 ! this is not a true fold; contains at least two very long antiparallel helices
99472 ! complexed with BtuB
64600 ! active form is a dimer
58106 ! long antiparallel four helical-bundle structure
64604 ! antiparallel right-handed coiled-coil
75708 ! dimerizes with the formation of a 4-helical bundle
72752 ! complexed with CheY
75712 ! dimerizes via a CxxC motif in the loop, zinc-hook
69989 ! left-handed antiparallel coiled-coil; dimerizes with the formation of a 4-helical bundle
66462 ! CASP4
103657 ! triple coiled coil; dimerizes in a six-helical bundle
103658 ! sensor of membrane curvature
111479 ! antiparallel coiled-coil in the crystals
106356 !SQ Q811U4 660-735
58112 ! tetrameric antiparallel coiled coil, closed in a circuit
58115 ! individual chains can form an up-and-down bundles
82935 ! segmented tetrameric parallel coiled coil
77743 ! a lipid surrogate complex
96623 ! tRNA model fitted into the cryo-EM map of 70S ribosome in the pre-translocational state
96627 ! S12, sh44, lh69 and srl separately fitted into the cryo-EM map of EF-Tu ternary complex
96886 ! L11 with 58nts of 23s rRNA fitted into the cryo-em map of the 70S ribosome
96888 ! L11 with 58nts of 23s rRNA fitted into the cryo-em map of EF-Tu ternary complex
88190 ! 30S subunit; the coordinates of 50S subunit in 1pnu
88243 ! 30S subunit; the coordinates of 50S subunit in 1pny
88223 ! 50S subunit; the coordinates of 30S subunit in 1pns
88276 ! 50S subunit; the coordinates of 30S subunit in 1pnx
106259 !SQ NA # ECM low resolution structure; the RRF-binding site 
106256 !SQ NA # ECM low resolution structure; the RRF-binding site 
96622 ! tRNA model fitted into the cryo-EM map of EF-Tu ternary complex
96628 ! EF-Tu/kirromycin model fitted into the cryo-EM map of EF-Tu ternary complex
79178 ! Fitting the ternary complex of EF-TU/tRNA/GTP in the cryo-EM map
63236 ! Fitting of L11 protein and elongation factor G (EF-G) in the cryo-EM map
63239 ! Fitting of L11 and EF-G domains G' and V in the cryo-EM map
74257 ! Fitting of the anticodon loop of tRNA (nucleotide 26-42) in the cryo-EM map
45826 ! tRNA positions during the elongation cycle
63240 ! Fitting of L11 in the cryo-EM map
79149 ! Docking of the modified RF2 x-ray structure
79279 ! also include low case chains a;b;c;d;e;f;g;h;l;m;n;o;p;q;r;s;t;u;v;w;x ! termination complex with release factor 2
87868 ! 50S subunit fit in the cryo-EM map of 70S ribosome
87838 ! 30S subunit fit in the cryo-EM map of 70S ribosome
87895 ! 50S subunit fit in the cryo-EM map of 70S ribosome
87940 ! 30S subunit fit in the cryo-EM map of 70S ribosome
88161 ! domain-wise fitting of the crystal structure of T. thermophilus EF-G in the cryo-EM map of 70S ribosome
88162 ! S12, L11 proteins and p-tRNA aligned to the cryo-EM map
88165 ! S12, L11 proteins and E-site tRNA aligned to the cryo-EM map
74239 ! Fitting of EF-TU and tRNA in the cryo-EM map
105170 !MQ NA # low resolution complex structure ! 40S subunit; the 60S subunit is in 1S1I
105200 !MQ NA # low resolution complex structure ! 60S subunit; the 40S subunit is in 1S1H
109118 !SQ NA # a low-resolution ribosomal 50S structure in complex with the trigger factor
45833 ! complexed with a 13 bp minihelix- puromycin compound
45834 ! complexed with r(CC)-dA-puromycin
80554 ! complexed with a tRNA acceptor stem mimic (asm)
80584 ! CA-atoms only for the ribosomal protein structures
80549 ! complexed with a tRNA acceptor stem mimic (asm) and the antibiotic sparsomycin
87140 ! complexed with troleandomycin macrolide antibiotic
94401 ! complexed with the telithromycin ketolide antibiotic
86343 ! CA-atoms only for the ribosomal protein structures
105728 !SQ NA # low resolution structure of ribosone 50S subunit
86312 ! CA-atoms only for the ribosomal protein structures
80550 ! complexed with the antibiotic sparsomycin
80551 ! complexed with a short substrate analog accpuromycin (accp)
45884 ! RecA hexamer model
79724 ! model for active RecA filament
58148 ! not a true family
58157 ! not a true family
58160 ! there is a higher resolution structure of Thermosynechococcus elongatus photosystem II </i>(<a href="../pdb.cgi?pdb=1s5l">1s5l</a>)<i>; however, PDB entry 1S5L designates protein chains by both upper case and lower case letters creating problems with its processing and presentation; there are two copies of the photosystem II complex: one with the upper case chains and the other with lower case chains
103669 ! light-harvesting chlorophyll a/b  protein complex with an icosahedral assembly
103670 ! a higher resolution structure of a homologous protein is also available, PDB entry 1RWT
103671 ! RNA-dependent RNA-polymerase
94132 ! Cryo-EM reconstruction; envelope proteins E (chains A, B and C) and M (chains D, E and F)
72064 ! major envelope protein E; sequence of the tick-borne encephalitis virus protein (see 1svb)
85362 ! immature particles; major envelope protein E; sequence of the tick-borne encephalitis virus protein (see 1svb)
91747 ! immature particles; major envelope protein E; sequence of the tick-borne encephalitis virus protein (see 1svb)
107023 !SQ NA # EM reconstruction
94535 ! fitting of baseplate structural protein gp11
94553 ! fitting of short tail fiber protein gp12
94556 ! fitting of baseplate structural protein gp27
94559 ! fitting of tail-associated lysozyme gp5
94571 ! fitting of baseplate structural protein gp8
94589 ! fitting of baseplate structural protein gp9
73759 ! holoenzyme at 4 Angstrom resolution
73771 ! holoenzyme/fork-junction promoter DNA complex at 6.5 Angstrom resolution
95040 ! complexed with transcription elongation factor S-II 
97115 ! complexed with transcription elongation factor TFIIB 
98845 ! strand separated elongation complex
46000 ! Pseudomonas aeruginosa ps-1-modified fragment
71166 ! in ATP-form
61945 ! Cryo-EM structure
98895 ! cryo-EM structure
65528 ! Cryo-EM structure of GroES-ADP(7)-GroEL-ATP(7)
65491 ! Cryo-EM structure of apo GroEL
65505 ! Cryo-EM structure of GroEL-ATP complex
109215 !SQ NA # low-resolution complex structure of known components
107505 !SQ NA # low-resolution structure ! there are upper case and lower case identifiers in this PDB entry that may cause processing and display errors; the upper case identifiers are for the toxin chains and the lower case identifiers (a;b;c;d;e;f;g;h;i;j;k;l;m;o) are for the receptor chains
58200 ! this is not a true family
46015 ! old structure, probably contains a sequence error
46016 ! structure contains only differences to 1GRG
46019 ! low resolution, sequence unknown
46020 ! incorrect structure (see ref 1, PDB entry for the correct one)
46021 ! old incorrect structure
46024 ! unknown sequence of this structure was deduced by X-ray crystallography at atomic resolution
58235 ! different conformations
107068 !SQ NA # non-ribosomal biosynthesis peptide
107109 !SQ NA # non-ribosome synthesis; D-aminoacid containing peptide; Mini-gramicidin A
58243 ! peptide antibiotic
108181 !SQ P29559 # postranslationally modified peptide
100898 ! consists of a conserved, disulfide-containing N-terminal region (forming a beta-sheet) and a C-terminal helix 
58254 ! antibacterial peptide, bacteriocin
58251 ! contains beta-hairpin crosslinked by disulfide bridge(s)
58252 ! not a true superfamily
82959 ! horseshoe crab antimicrobial peptide
104966 !SQ NA # short peptide
64621 ! a cyclic antimicrobial defensin from rhesus macaque leukocytes
58266 ! Antimicrobial peptide derived from bovine lactoferrin
78600 ! hepcidin-20
78601 ! hepcidin-25
86682 ! an acyclic permutant
86683 ! an acyclic permutant
58268 ! antibiotic peptide
58269 ! not a true superfamily
59137 ! bound to phospholipid vesicles
58278 ! macrocyclic antimicrobial peptide; bacteriocin
105357 !SQ Q9X2V7 38-58 ! thermolysin digested peptide
94972 ! a lariat protoknot; different residue numbering from obsolete entries
111498 ! unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons
104382 !SQ O07623 9-43
58283 ! contains one alpha-helix
58284 ! this is not a true superfamily
105099 !SQ P68005
105100 !SQ P68005
58296 ! ten-residue peptide with one disulfide
85499 ! synthetic glucagon antagonist; (desHis1, desPhe6, Glu9)glucagon amide
68879 ! structure in a lipid-water interphase
70005 ! glucagone-like hormone
104090 !SQ Q9UHF0 81-90 # human TaxID: 9606
104674 !SQ O43612 34-66 
109542 !SQ P81861 
58307 ! single alpha helix
104024 !SQ P56029 2-20
58318 ! parasite of armyworm (<i>Pseudaletia separata</i>?)
46124 ! residues 33-55
46125 ! residues 34-50; bound to RNA
46121 ! residues 34-50
46122 ! residues 34-50; bound to RNA
62089 ! bound to RNA
46123 ! residues 33-55
46128 ! residues 68-81; bound to TAR RNA
46129 ! residues 65-81; bound to TAR RNA
58346 ! bound to its RNA aptamer target
46133 ! second domain
46134 ! third domain
46135 ! second domain
46136 ! third domain
73380 ! residues 34-51
73378 ! residues 34-51
73379 ! residues 34-51
46138 ! residues 52-96
46140 ! residues 13-33; in micelles
84879 ! residues 1-96; globular structure: an open 3-helical bundle
46142 ! residues 50-82
46137 ! residues 1-51
46139 ! residues 50-75
59501 ! residues 1-96; non-globular structure
46141 ! residues 59-86
58360 ! it is not a true family
84413 ! tandem inactivation domain (residues 1-75)
46149 ! CASP1
58376 ! alpha-helix
46150 ! residues 267-288
46151 ! residues 236-268
46173 ! D-Pro14 synthetic variant
58404 ! small disulfide-rich peptide
46178 ! Synthetic hydrophobic analogue
71540 ! Synthetic hydrophobic analogue
46179 ! residues 1-47
46180 ! residues 147-163
78293 ! residues 147-163
58430 ! 21-residue disulfide-bound peptide
58435 ! A-type receptor specific hypotensive hormone
46191 ! CA-atoms only, mutant protein sequence
58444 ! no or little secondary structure
58449 ! small disulfide-rich
46200 ! linear modified endothelin-1 agonist
46199 ! linear truncated endothelin-1 agonist
58459 ! short disulfide-bound peptide
58462 ! endogenous ligand to the HSE receptor
46207 ! uroguanylin-16
46208 ! uroguanylin-16
58464 ! disulfide-rich fold
58465 ! all apart omega class; it is not a true superfamily
58471 ! 13-16 residue peptide with 2 disulfides
46223 ! Synthetic antitoxic analog
79669 ! disulfide bond isomer
107920 !SQ Q86RB2 21-36
58495 ! gamma-carboxyglutamic acid (GLA)-rich peptide; active conformation may be stabilized by metal ions
46229 ! metal-free
58505 ! contains D-tryptophan
70081 ! an engineered contryphan cyclic peptide
70082 ! an engineered contryphan cyclic peptide
46234 ! an engineered contryphan cyclic peptide (motif cpxxpxc)
86387 ! contryphan-vn cis conformer
58507 ! hairpin of two short helices crosslinked with two disulfides
103729 ! antimicrobial peptide; consists of N-terminal proline-rich tail and C-terminal cysteine-rich domain
63138 ! bradykinin-penta-O-galloyl-D-glucopyranose complex
58519 ! the member of this family may be not related
92387 ! phosphorylated carboxy terminus (19 residues)
46240 ! intradiskal loop 1
46242 ! 2nd intradiskal loop
46241 ! third intradiskal loop
46243 ! amino terminus (residues 1-40)
46244 ! helix 7
105999 !SQ P07988 208-225,263-278 # mini-B: an N-terminal/C-terminal construct
104925 !SQ P07988 263-278 # coverage from PDB DBREF
104924 !SQ P07988 263-278 # coverage from PDB DBREF
58532 ! right-hand twisted coiled coil
46259 ! residues 9-26, 52-79
58538 ! M3 transmembrane segment
86407 ! the closed state structure by solid state NMR spectroscopy
90285 ! amphipathic helix; this region is partly disordered in the crystal structure of the whole protein </i>(<a href="../pdb.cgi?pdb=d1gl">d1gl</a>)<i>a CH F
94759 ! 6th transmembrane helix 
91371 ! 2nd transmembrane helix 
104832 !SQ P27958 1972-2003
104831 !SQ P27958 1972-2003
104833 !SQ P27958 1972-2003
104835 !SQ P27958 1972-2003
104834 !SQ P27958 1972-2003
46286 ! cytoplasmic domain residues 1-25
46289 ! peptide based on mimic mung bean trypsin inhibitor
76231 ! the antitryptic reactive site loop
60963 ! reactive site loop sequence
86679 ! residues 1-79
61788 ! residues 13-79
105845 !SQ P02655 23-101 ! structure in dodecyl phosphocholine
46301 ! residues 44-79
81093 ! residues 1-16
46312 ! residues 1-40
76974 ! residues 1-42
46313 ! residues 1-28
46314 ! residues 1-40
46311 ! residues 1-28
46317 ! residues 1-28
46310 ! residues 1-28
46316 ! residues 10-35
104643 !SQ P05067 696-706 # coverage from PDB
46309 ! residues 25-35
46315 ! residues 1-40
104621 !SQ P05067 696-706 # coverage from PDB
80660 ! residues 1-28
58617 ! has different conformations in free and antibody-bound forms
18264 ! residues 255-316
58637 ! interact with proto-oncogene tyrosine-protein kinase lck
95962 ! residues 421-458
46327 ! residues 428-444 (403-419 in old numbering)
103751 ! zinc ion-mediated interaction
58652 ! not a true family
46332 ! residues 46-87 bound to Gi1 alpha
46333 ! residues 1-25
46334 ! anchor domain; res. 2-57
46335 ! anchor domain; res. 2-57
46336 ! consensus peptide; antibody-bound
80544 ! antibody-bound
80543 ! antibody-bound
66474 ! bound to dpc micelles
66475 ! bound to dpc micelles
76752 ! cyclic analogue
82983 ! 2f5 mab epitope
71120 ! ligand a1
71135 ! ligand d18
71127 ! ligand a22
71134 ! ligand d16
58705 ! protein-dimerization inhibitor based on a fragment from the enzyme sequence
58710 ! as bound to the large subunit
58715 ! as bound to a monoclonal antibody
46349 ! the retro-inverso analogue
46350 ! the retro-inverso analogue
46351 ! the retro-inverso analogue
46355 ! bound to the Smad2 MH2 domain
79218 ! bound to the Smad3 MH2 domain
76573 ! complexed with FIH1
76575 ! complexed with FIH1
73686 ! complexed with TAZ1 domain of mouse CBP
73535 ! complexed with TAZ1 domain of human CBP
87777 ! complexed with TAZ1 domain of mouse CBP
97249 ! complexed with TAZ1 domain of mouse CBP
104394 !SQ O43792 687-700
106853 !SQ O43792 687-697
79773 ! bound to Rad51
46356 ! bound to CDC42Hs
46357 ! bound to CDC42Hs
106360 !SQ P07293 358-374 ! complexed with a Cab2 domain
106213 !SQ Q13936 428-443
108913 !SQ P22002 452-476
103753 ! selectively cytotoxic to cancer cells
46365 ! as bound to importin-beta
46369 ! as bound to botulinum neurotoxin type b catalytic domain
46370 ! peptide 1-10
59433 ! Solution structure in the presence of phosphatidylinositol 4,5- bisphosphate
70020 ! actin-binding peptide
105924 !SQ O97428 10-34
60464 ! residues 132-152; receptor-bound conformation of p
65701 ! 49 aa presequence
65702 ! 26 aa presequence
61454 ! the third extracellular loop; residues 329-357
77694 ! the third extracellular loop; residues 352-379
62848 ! an acyclic permutant
98510 ! 21-mer peptide, residues 133-155
65075 ! 26-mer peptide, residues 145-169
74431 ! 26-mer peptide, residues 145-169
92796 ! residues 61-68; one 8-aa repeat
92797 ! residues 61-84; three 8-aa repeats
71088 ! T7 novispirin
71086 ! ovispirin-1
71087 ! G10 novispirin
79864 ! SS-cyclized
79388 ! SS-cyclized
76872 ! TFE-induced structure
78245 ! bound to g(alpha)i
78246 ! bound to g(alpha)i
64661 ! two alpha-helical segments visible in the crystal structure
105326 !SQ P15825
90304 ! amphipathic helix
86524 ! C-terminal UIM
95514 ! tandem repeat of two UIMs
95515 ! N-terminal UIM; complexed with ubiquitin
103766 ! a protease inhibitor containing two ester linkages
109426 !SQ Q5USN7 150-177
109427 !SQ P58455
105280 !SQ Q8TBM1 358-380
105278 !SQ Q05195 6-21 # structure of the B-HLH-Z region (57-136) is also known (1nlw chains A and D; scop_sp: 81753)
104917 !SQ P36941 384-408
105532 !SQ O14745 321-358
103777 ! beta(2)-alpha-beta-alpha-beta(2); 2 layers: a/b; antiparallel beta-sheet: order 21354
103782 ! binds ADP; contains zinc-binding site similar to that of the transcription factor GATA-1
58794 ! dimeric coiled coil
58796 ! myosin II heavy chain fused to alpha-actinin spectrin-like repeats 1 and 2
46381 ! racemic p1bar form
46385 ! p1 form
83012 ! packing of helices in octamer is similar to that of the Uteroglobin-like dimer (see 2utg)
76790 ! high resolution structure
103784 ! contains a discontinuity in the repeating tripeptide sequence
85504 ! foldon is a trimerisation domain of T4 fibritin
108405 !SQ NA # designed sequence
108400 !SQ NA # designed sequence
108354 !SQ NA # designed sequence
100905 ! not a true family
46408 ! CASP2
58834 ! this is not a true family
103787 ! single-chain four-helical protein
58837 ! dimeric alpha-hairpin fold
104036 !SQ gi|9955104|pdb|1EC5|A # designed sequence
58839 ! not a true fold: both possible topologies are created
75767 ! <i>de novo</i> designed protein model of radical enzymes
58849 ! Designed sequence (EQLLKALEFLLKELLEKL),
46429 ! CASP3
70056 ! a chimeric peptide model of tropomyosin and GCN4 coiled coils
58861 ! original sequence taken from the third zinc finger domain of the human transcriptional repressor protein yy1
60223 ! clone 6
60221 ! clone 2
104952 !SQ NA # designed peptide
104953 !SQ NA # designed peptide
73644 ! bound to Fc fragment of rituximab IgG1
87318 ! minimized version of protein A called mini-Z (Z34c)
87330 ! minimized version of protein A called mini-Z (Z34c)
46435 ! disulfide-stabilized minidomain
46434 ! disulfide-stabilized minidomain
46436 ! phage-selected minidomain
46437 ! phage-selected minidomain
106665 !SQ gi|49259279|pdb|1T8J|A # designed sequence
105812 !SQ NA # designed miniprotein
105818 !SQ NA # designed miniprotein
105816 !SQ NA # designed miniprotein
104534 !SQ NA # De novo design
90309 ! alpha-helical arrays from an idealized TPR motif
46448 ! bound to the receptor extracellular domains
58911 ! consensus sequence from a number of sources
88375 ! complex with RS20 peptide, chain B
46451 ! complex with RS20 peptide
88374 ! complex with RS20 peptide, chains B and D
106058 !SQ gi|49259167|pdb|1SVX|A # designed sequence
58923 ! interacting with the hiv-1 envelope glycoprotein
60032 ! isomer-a
60031 ! isomer-b
104951 !SQ NA # designed peptide
64704 ! not a true superfamily
73925 ! Non-native conformation
75792 ! de novo designed eight-stranded beta-sheet assembled using a disulfide bond
71943 ! B4dimer A variant
75794 ! designed water soluble four-stranded antiparallel beta-sheet protein
107025 !SQ NA # designed peptide
108717 !SQ NA # designed sequence