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

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2078560Fold 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. 2081496Superfamily c.1.8: (Trans)glycosidases [51445] (15 families) (S)
  5. 2081497Family c.1.8.1: Amylase, catalytic domain [51446] (26 protein domains)
    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. 2081613Protein Bacterial alpha-amylase [51447] (10 species)
  7. 2081621Species Bacillus sp. 707 [TaxId:1416] [117366] (4 PDB entries)
    Uniprot P19571 38-518
  8. 2081622Domain 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 (more details), 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: (download)

>d2d3na2 c.1.8.1 (A:5-398) Bacterial alpha-amylase {Bacillus sp. 707 [TaxId: 1416]}

SCOPe Domain Coordinates for d2d3na2:

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(The format of our PDB-style files is described here.)

Timeline for d2d3na2:

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