SCOP 1.71: Domain d1e3za2: 1e3z A:1-393

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

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (32 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] (13 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (24 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] (8 species)

7. Species Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis) [TaxId:1390] [63903] (4 PDB entries)
   the N-terminal 300 residues are from B. amyloliquefaciens

8. Domain d1e3za2: 1e3z A:1-393 [59214]
   Other proteins in same PDB: d1e3za1
   complexed with ca, cmn, g6d, glc, na

Details for d1e3za2

PDB Entry: 1e3z, 1.93 Å

PDB Description: acarbose complex of chimaeric amylase from b. amyloliquefaciens and b. licheniformis at 1.93a

SCOP Domain Sequences for d1e3za2:

Sequence; same for both SEQRES and ATOM records:

>d1e3za2 c.1.8.1 (A:1-393) Bacterial alpha-amylase {Chimera (Bacillus amyloliquefaciens) and (Bacillus licheniformis)}
vngtlmqyfewytpndgqhwkrlqndaehlsdigitavwippaykglsqsdngygpydly
dlgefqqkgtvrtkygtkselqdaigslhsrnvqvygdvvlnhkagadatedvtavevnp
anrnqetseeyqikawtdfrfpgrgntysdfkwhwyhfdgadwdesrkisrifkfrgegk
awdwevssengnydylmyadvdydhpdvvaetkkwgiwyanelsldgfridaakhikfsf
lrdwvqavrqatgkemftvaeywqnnagklenylnktsfnqsvfdvplhfnlqaassqgg
gydmrkllngtvvskhplksvtfvdnhdtqpgqslestvqtwfkplayafiltresgypq
vfygdmygtkgdsqreipalkhkiepilkarkq

Timeline for d1e3za2:

• d1e3za2 first appeared in SCOP 1.57
  
• d1e3za2 appears in SCOP 1.69
  
• d1e3za2 appears in SCOP 1.73
  
• d1e3za2 appears in the current release, SCOPe 2.08