SCOPe 2.08: Domain d1g1yb3: 1g1y B:121-502

Lineage for d1g1yb3 (1g1y B:121-502)

1. Root: SCOPe 2.08

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

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 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 Maltogenic amylase, central domain [51465] (4 species)
   contains an additional N-terminal domain

7. Species Thermoactinomyces vulgaris, TVAII [TaxId:2026] [51467] (12 PDB entries)

8. Domain d1g1yb3: 1g1y B:121-502 [60215]
   Other proteins in same PDB: d1g1ya1, d1g1ya2, d1g1yb1, d1g1yb2
   has additional subdomain(s) that are not in the common domain

Details for d1g1yb3

PDB Entry: 1g1y, 3 Å

PDB Description: crystal structure of alpha-amylase ii (tvaii) from thermoactinomyces vulgaris r-47 and beta-cyclodextrin complex

PDB Compounds: (B:) alpha-amylase II

SCOPe Domain Sequences for d1g1yb3:

Sequence; same for both SEQRES and ATOM records:

>d1g1yb3 c.1.8.1 (B:121-502) Maltogenic amylase, central domain {Thermoactinomyces vulgaris, TVAII [TaxId: 2026]}
vfttpewakeaviyqifperfangdpsndppgteqwakdarprhdsfyggdlkgvidrlp
yleelgvtalyftpifaspshhkydtadylaidpqfgdlptfrrlvdeahrrgikiilda
vfnhagdqffafrdvlqkgeqsrykdwffiedfpvsktsrtnyetfavqvpampklrten
pevkeylfdvarfwmeqgidgwrldvanevdhafwrefrrlvkslnpdalivgaiwhdas
gwlmgdqfdsvmnylfresvirffatgeihaerfdaeltrarmlypeqaaqglwnlldsh
dterfltscggneakfrlavlfqmtylgtpliyygdeigmagatdpdcrrpmiweekeqn
rglfefykelirlrhrlasltr

Timeline for d1g1yb3:

• d1g1yb3 first appeared in SCOP 1.57
  
• d1g1yb3 appears in SCOPe 2.07