SCOPe 2.03: Domain d1vepa2: 1vep A:1-417

Lineage for d1vepa2 (1vep A:1-417)

1. Root: SCOPe 2.03

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold 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. 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 beta-amylase [51485] (1 species)
   protein contains additional starch-binding domain

7. Species Bacillus cereus [TaxId:1396] [51486] (14 PDB entries)

8. Domain d1vepa2: 1vep A:1-417 [120028]
   Other proteins in same PDB: d1vepa1
   automatically matched to d1b90a2
   complexed with ca

Details for d1vepa2

PDB Entry: 1vep, 2.06 Å

PDB Description: crystal structure analysis of triple (t47m/y164e/t328n)/maltose of bacillus cereus beta-amylase at ph 6.5

PDB Compounds: (A:) beta-amylase

SCOPe Domain Sequences for d1vepa2:

Sequence; same for both SEQRES and ATOM records:

>d1vepa2 c.1.8.1 (A:1-417) Bacterial beta-amylase {Bacillus cereus [TaxId: 1396]}
avngkgmnpdykaylmaplkkipevtnwetfendlrwakqngfyaimvdfwwgdmekngd
qqfdfsyaqrfaqsvknagmkmipiisthqcggnvgddcnvpipswvwnqksddslyfks
etgtvnketlnplasdvirkeygelytafaaamkpykdviakielsggpagelrypsytt
sdgtgypsrgkfqaytefakskfrlwvlnkygslnevnkawgtkliselailppsdgeqf
lmngylsmygkdylewyqgilenhtkligelahnafdttfqvpigakiagvhwqynnpti
phgaekpagyndyshlldafksakldvnftclemtdkgsypeysmpktlvqniatlanek
givlngenalsigneeeykrvaemafnynfagftllryqdvmynnslmgkfkdllgv

Timeline for d1vepa2:

• d1vepa2 first appeared in SCOP 1.73
  
• d1vepa2 appears in SCOPe 2.02
  
• d1vepa2 appears in SCOPe 2.04
  
• d1vepa2 appears in the current release, SCOPe 2.08