SCOPe 2.05: Domain d1hnya2: 1hny A:1-403

Lineage for d1hnya2 (1hny A:1-403)

1. Root: SCOPe 2.05

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. 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

4. Superfamily c.1.8: (Trans)glycosidases [51445] (15 families)

5. 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

6. Protein Animal alpha-amylase [51458] (3 species)
   contains Ca2+-binding subdomain, residues 100-170

7. Species Human (Homo sapiens) [TaxId:9606] [51460] (49 PDB entries)
   Uniprot P04746 16-511 ! SQ 04746

8. Domain d1hnya2: 1hny A:1-403 [28756]
   Other proteins in same PDB: d1hnya1
   complexed with ca, cl

Details for d1hnya2

PDB Entry: 1hny, 1.8 Å

PDB Description: the structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes

PDB Compounds: (A:) human pancreatic alpha-amylase

SCOPe Domain Sequences for d1hnya2:

Sequence; same for both SEQRES and ATOM records:

>d1hnya2 c.1.8.1 (A:1-403) Animal alpha-amylase {Human (Homo sapiens) [TaxId: 9606]}
eyspntqqgrtsivhlfewrwvdialecerylapkgfggvqvsppnenvaiynpfrpwwe
ryqpvsyklctrsgnedefrnmvtrcnnvgvriyvdavinhmcgnavsagtsstcgsyfn
pgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrltglldlalekdyvrskia
eymnhlidigvagfrldaskhmwpgdikaildklhnlnsnwfpagskpfiyqevidlgge
pikssdyfgngrvtefkygaklgtvirkwngekmsylknwgegwgfvpsdralvfvdnhd
nqrghgaggasiltfwdarlykmavgfmlahpygftrvmssyrwprqfqngndvndwvgp
pnnngvikevtinpdttcgndwvcehrwrqirnmvifrnvvdg

Timeline for d1hnya2:

• d1hnya2 first appeared (with stable ids) in SCOP 1.55, called d1hny_2
  
• d1hnya2 appears in SCOPe 2.04
  
• d1hnya2 appears in SCOPe 2.06
  
• d1hnya2 appears in the current release, SCOPe 2.08