SCOPe 2.03: Domain d1ynyb1: 1yny B:2-52,B:385-460

Lineage for d1ynyb1 (1yny B:2-52,B:385-460)

1. Root: SCOPe 2.03

2. Class b: All beta proteins [48724] (174 folds)

3. Fold b.92: Composite domain of metallo-dependent hydrolases [51337] (1 superfamily)
   pseudobarrel; mixed sheet of 7 strand folded upon itself and "buckled" by two beta-turns

4. Superfamily b.92.1: Composite domain of metallo-dependent hydrolases [51338] (11 families)
   this domain is interrupted by the catalytic beta/alpha barrel domain

5. Family b.92.1.3: Hydantoinase (dihydropyrimidinase) [75044] (5 proteins)

6. Protein D-hydantoinase [75045] (4 species)

7. Species Bacillus sp. AR9 [TaxId:301298] [141682] (1 PDB entry)
   Uniprot Q5DLU2 2-52,385-460

8. Domain d1ynyb1: 1yny B:2-52,B:385-460 [123766]
   Other proteins in same PDB: d1ynya2, d1ynyb2
   automated match to d1ynya1
   complexed with mn

Details for d1ynyb1

PDB Entry: 1yny, 2.3 Å

PDB Description: molecular structure of d-hydantoinase from a bacillus sp. ar9: evidence for mercury inhibition

PDB Compounds: (B:) D-hydantoinase

SCOPe Domain Sequences for d1ynyb1:

Sequence; same for both SEQRES and ATOM records:

>d1ynyb1 b.92.1.3 (B:2-52,B:385-460) D-hydantoinase {Bacillus sp. AR9 [TaxId: 301298]}
kkwirggtvvtaadtyqadvliegervvaighqlsvngaeeidatgcyvipXiavgsdad
ivifdphvkrtlsvethhmnvdynpfegmevygevvsvlsrgsfvvrdkqfvgqagsgqy
ikrttfeq

Timeline for d1ynyb1:

• d1ynyb1 first appeared in SCOP 1.73
  
• d1ynyb1 appears in SCOPe 2.02
  
• d1ynyb1 appears in SCOPe 2.04
  
• d1ynyb1 appears in the current release, SCOPe 2.08