Lineage for d1e3za2 (1e3z A:1-393)

  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. 2081638Species Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis) [TaxId:1390] [63903] (4 PDB entries)
    the N-terminal 300 residues are from B. amyloliquefaciens
  8. 2081641Domain d1e3za2: 1e3z A:1-393 [59214]
    Other proteins in same PDB: d1e3za1
    complexed with aci, ca, na

Details for d1e3za2

PDB Entry: 1e3z (more details), 1.93 Å

PDB Description: acarbose complex of chimaeric amylase from b. amyloliquefaciens and b. licheniformis at 1.93a
PDB Compounds: (A:) alpha-amylase

SCOPe Domain Sequences for d1e3za2:

Sequence; same for both SEQRES and ATOM records: (download)

>d1e3za2 c.1.8.1 (A:1-393) Bacterial alpha-amylase {Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis) [TaxId: 1390]}

SCOPe Domain Coordinates for d1e3za2:

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Timeline for d1e3za2:

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