SCOPe 2.03: Domain d1ynya1: 1yny A:2-52,A:385-460

Lineage for d1ynya1 (1yny A:2-52,A: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 d1ynya1: 1yny A:2-52,A:385-460 [123764]
   Other proteins in same PDB: d1ynya2, d1ynyb2
   complexed with mn

Details for d1ynya1

PDB Entry: 1yny, 2.3 Å

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

PDB Compounds: (A:) D-hydantoinase

SCOPe Domain Sequences for d1ynya1:

Sequence, based on SEQRES records:

>d1ynya1 b.92.1.3 (A:2-52,A:385-460) D-hydantoinase {Bacillus sp. AR9 [TaxId: 301298]}
kkwirggtvvtaadtyqadvliegervvaighqlsvngaeeidatgcyvipXiavgsdad
ivifdphvkrtlsvethhmnvdynpfegmevygevvsvlsrgsfvvrdkqfvgqagsgqy
ikrttfeq

Sequence, based on observed residues (ATOM records):

>d1ynya1 b.92.1.3 (A:2-52,A:385-460) D-hydantoinase {Bacillus sp. AR9 [TaxId: 301298]}
kkwirggtvvtaadtyqadvliegervvaighqgaeeidatgcyvipXiavgsdadivif
dphvkrtlsvethhmnvdynpfegmevygevvsvlsrgsfvvrdkqfvgqagsgqyikrt
tfeq

Timeline for d1ynya1:

• d1ynya1 first appeared in SCOP 1.73
  
• d1ynya1 appears in SCOPe 2.02
  
• d1ynya1 appears in SCOPe 2.04
  
• d1ynya1 appears in the current release, SCOPe 2.08