SCOPe 2.08: Domain d2d3na2: 2d3n A:5-398

Lineage for d2d3na2 (2d3n A:5-398)

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 Bacterial alpha-amylase [51447] (10 species)

7. Species Bacillus sp. 707 [TaxId:1416] [117366] (4 PDB entries)
   Uniprot P19571 38-518

8. Domain d2d3na2: 2d3n A:5-398 [131213]
   Other proteins in same PDB: d2d3na1
   automated match to d1wpca2
   complexed with ca, glc, na

Details for d2d3na2

PDB Entry: 2d3n, 1.9 Å

PDB Description: crystal structure of maltohexaose-producing amylase from bacillus sp.707 complexed with maltohexaose

PDB Compounds: (A:) Glucan 1,4-alpha-maltohexaosidase

SCOPe Domain Sequences for d2d3na2:

Sequence; same for both SEQRES and ATOM records:

>d2d3na2 c.1.8.1 (A:5-398) Bacterial alpha-amylase {Bacillus sp. 707 [TaxId: 1416]}
tngtmmqyfewylpndgnhwnrlnsdasnlkskgitavwippawkgasqndvgygaydly
dlgefnqkgtvrtkygtrsqlqaavtslknngiqvygdvvmnhkggadatemvravevnp
nnrnqevtgeytieawtrfdfpgrgnthssfkwrwyhfdgvdwdqsrrlnnriykfrghg
kawdwevdtengnydylmyadidmdhpevvnelrnwgvwytntlgldgfridavkhikys
ftrdwinhvrsatgknmfavaefwkndlgaienylqktnwnhsvfdvplhynlynasksg
gnydmrnifngtvvqrhpshavtfvdnhdsqpeealesfveewfkplayaltltreqgyp
svfygdyygipthgvpamrskidpilearqkyay

Timeline for d2d3na2:

• d2d3na2 first appeared in SCOP 1.73
  
• d2d3na2 appears in SCOPe 2.07