SCOPe 2.01: Domain d1gkqd2: 1gkq D:55-389

Lineage for d1gkqd2 (1gkq D:55-389)

1. Root: SCOPe 2.01

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.1.9: Metallo-dependent hydrolases [51556] (19 families)
   the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
   has transition metal ions bound inside the barrel

5. Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (5 proteins)

6. Protein D-hydantoinase [75074] (4 species)

7. Species Thermus sp. [TaxId:275] [75075] (2 PDB entries)

8. Domain d1gkqd2: 1gkq D:55-389 [70250]
   Other proteins in same PDB: d1gkqa1, d1gkqb1, d1gkqc1, d1gkqd1
   complexed with zn

Details for d1gkqd2

PDB Entry: 1gkq, 2.6 Å

PDB Description: d-hydantoinase (dihydropyrimidinase) from thermus sp. in space group p212121

PDB Compounds: (D:) hydantoinase

SCOPe Domain Sequences for d1gkqd2:

Sequence; same for both SEQRES and ATOM records:

>d1gkqd2 c.1.9.6 (D:55-389) D-hydantoinase {Thermus sp. [TaxId: 275]}
fidphvhiylpfmatfakdthetgskaalmggtttyiemccpsrnddalegyqlwkskae
gnsycdytfhmavskfdektegqlreivadgissfkiflsyknffgvddgemyqtlrlak
elgvivtahcenaelvgrlqqkllsegktgpewhepsrpeaveaegtarfatflettgat
gyvvhlsckpaldaamaakargvpiyiesviphflldktyaerggveamkyimspplrdk
rnqkvlwdalaqgfidtvgtdhcpfdteqkllgkeaftaipngipaiedrvnllytygvs
rgrldihrfvdaastkaaklfglfprkgtiavgsd

Timeline for d1gkqd2:

• d1gkqd2 first appeared in SCOP 1.61
  
• d1gkqd2 appears in SCOP 1.75
  
• d1gkqd2 appears in SCOPe 2.02
  
• d1gkqd2 appears in the current release, SCOPe 2.08