![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
![]() | Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies) contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites |
![]() | Superfamily c.1.8: (Trans)glycosidases [51445] (15 families) ![]() |
![]() | Family c.1.8.1: Amylase, catalytic domain [51446] (26 proteins) 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 |
![]() | Protein Animal alpha-amylase [51458] (3 species) contains Ca2+-binding subdomain, residues 100-170 |
![]() | Species Human (Homo sapiens) [TaxId:9606] [51460] (55 PDB entries) Uniprot P04746 16-511 ! SQ 04746 |
![]() | Domain d1u33a2: 1u33 A:1-403 [107633] Other proteins in same PDB: d1u33a1 complexed with ca, cl, lm2, nag |
PDB Entry: 1u33 (more details), 1.95 Å
SCOPe Domain Sequences for d1u33a2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1u33a2 c.1.8.1 (A:1-403) Animal alpha-amylase {Human (Homo sapiens) [TaxId: 9606]} eyspntqqgrtsivhlfewrwvdialecerylapkgfggvqvsppnenvaiynpfrpwwe ryqpvsyklctrsgnedefrnmvtrcnnvgvriyvdavinhmcgnavsagtsstcgsyfn pgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrltglldlalekdyvrskia eymnhlidigvagfrldaskhmwpgdikaildklhnlnsnwfpagskpfiyqevidlgge pikssdyfgngrvtefkygaklgtvirkwngekmsylknwgegwgfvpsdralvfvdnhd nqrghgaggasiltfwdarlykmavgfmlahpygftrvmssyrwprqfqngndvndwvgp pnnngvikevtinpdttcgndwvcehrwrqirnmvifrnvvdg
Timeline for d1u33a2: