![]() | Class c: Alpha and beta proteins (a/b) [51349] (141 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] (14 families) ![]() |
![]() | Family c.1.8.1: Amylase, catalytic domain [51446] (24 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] (33 PDB entries) |
![]() | Domain d1xh2a2: 1xh2 A:1-403 [121994] Other proteins in same PDB: d1xh2a1 automatically matched to d1c8qa2 complexed with are, ca, cl, nag; mutant |
PDB Entry: 1xh2 (more details), 2.2 Å
SCOP Domain Sequences for d1xh2a2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1xh2a2 c.1.8.1 (A:1-403) Animal alpha-amylase {Human (Homo sapiens) [TaxId: 9606]} eyspntqqgrtsivhlfewrwvdialecerylapkgfggvqvsppnenvaiynpfrpwwe ryqpvsyklctrsgnedefrnmvtrcnnvgvriyvdavinhmcgnavsagtsstcgsyfn pgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrltglldlalekdyvrskia eymnhlidigvagfrldaskhmwpgdikaildklhnlnsnwfpagskpfiyqevidlgge pikssdyfgngrvtefkygaklgtvirkwngekmsylknwgegwgfvpsdralvfvdshd nqrghgaggasiltfwdarlykmavgfmlahpygftrvmssyrwprqfqngndvndwvgp pnnngvikevtinpdttcgndwvcehrwrqirnmvifrnvvdg
Timeline for d1xh2a2: