SCOP 1.69: Domain d1v3ma4: 1v3m A:1-406

Lineage for d1v3ma4 (1v3m A:1-406)

1. Root: SCOP 1.69

2. Class c: Alpha and beta proteins (a/b) [51349] (136 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (31 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] (11 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 Cyclodextrin glycosyltransferase [51452] (5 species)
   contains two more all-beta domains, one is Immunoglobulin-like and the other is trasthyretin-like

7. Species Alkalophilic bacillus sp., strain 1011 [51456] (8 PDB entries)

8. Domain d1v3ma4: 1v3m A:1-406 [108332]
   Other proteins in same PDB: d1v3ma1, d1v3ma2, d1v3ma3, d1v3mb1, d1v3mb2, d1v3mb3

Details for d1v3ma4

PDB Entry: 1v3m, 2 Å

PDB Description: crystal structure of f283y mutant cyclodextrin glycosyltransferase complexed with a pseudo-tetraose derived from acarbose

SCOP Domain Sequences for d1v3ma4:

Sequence; same for both SEQRES and ATOM records:

>d1v3ma4 c.1.8.1 (A:1-406) Cyclodextrin glycosyltransferase {Alkalophilic bacillus sp., strain 1011}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgsctnlrlycggdwqgiink
indgyltgmgitaiwisqpveniysvinysgvnntayhgywardfkktnpaygtmqdfkn
lidtahahnikviidfapnhtspassddpsfaengrlydngnllggytndtqnlfhhygg
tdfstiengiyknlydladlnhnnssvdvylkdaikmwldlgvdgirvdavkhmpfgwqk
sfmatinnykpvftfgewflgvneispeyhqfanesgmslldyrfaqkarqvfrdntdnm
yglkamlegsevdyaqvndqvtfidnhdmerfhtsngdrrkleqalaftltsrgvpaiyy
gseqymsggndpdnrarlpsfsttttayqviqklaplrksnpaiay

Timeline for d1v3ma4:

• d1v3ma4 is new in SCOP 1.69
  
• d1v3ma4 appears in SCOP 1.71
  
• d1v3ma4 appears in the current release, SCOPe 2.08