SCOP 1.71: Domain d1dtua4: 1dtu A:1-406

Lineage for d1dtua4 (1dtu A:1-406)

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 Cyclodextrin glycosyltransferase [51452] (5 species)
   contains two more all-beta domains, one is Immunoglobulin-like and the other is trasthyretin-like

7. Species Bacillus circulans, different strains [TaxId:1397] [51453] (36 PDB entries)

8. Domain d1dtua4: 1dtu A:1-406 [28734]
   Other proteins in same PDB: d1dtua1, d1dtua2, d1dtua3
   complexed with aci, ca, glc, gld; mutant

Details for d1dtua4

PDB Entry: 1dtu, 2.4 Å

PDB Description: bacillus circulans strain 251 cyclodextrin glycosyltransferase: a mutant y89d/s146p complexed to an hexasaccharide inhibitor

SCOP Domain Sequences for d1dtua4:

Sequence; same for both SEQRES and ATOM records:

>d1dtua4 c.1.8.1 (A:1-406) Cyclodextrin glycosyltransferase {Bacillus circulans, different strains}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgtctnlrlycggdwqgiink
indgyltgmgvtaiwisqpveniysiindsgvnntayhgywardfkktnpaygtiadfqn
liaaahaknikviidfapnhtspaspdqpsfaengrlydngtllggytndtqnlfhhngg
tdfsttengiyknlydladlnhnnstvdvylkdaikmwldlgidgirmdavkhmpfgwqk
sfmaavnnykpvftfgewflgvnevspenhkfanesgmslldfrfaqkvrqvfrdntdnm
yglkamlegsaadyaqvddqvtfidnhdmerfhasnanrrkleqalaftltsrgvpaiyy
gteqymsggtdpdnraripsfststtayqviqklaplrkcnpaiay

Timeline for d1dtua4:

• d1dtua4 first appeared (with stable ids) in SCOP 1.55
  
• d1dtua4 appears in SCOP 1.69
  
• d1dtua4 appears in SCOP 1.73
  
• d1dtua4 appears in the current release, SCOPe 2.08