![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
![]() | Fold c.1: TIM beta/alpha-barrel [51350] (34 superfamilies) contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites |
![]() | 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 |
![]() | Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (5 proteins) automatically mapped to Pfam PF13147 |
![]() | Protein D-hydantoinase [75074] (4 species) |
![]() | Species Thermus sp. [TaxId:275] [75075] (2 PDB entries) |
![]() | Domain d1gkqc2: 1gkq C:55-389 [70248] Other proteins in same PDB: d1gkqa1, d1gkqb1, d1gkqc1, d1gkqd1 complexed with zn |
PDB Entry: 1gkq (more details), 2.6 Å
SCOPe Domain Sequences for d1gkqc2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1gkqc2 c.1.9.6 (C:55-389) D-hydantoinase {Thermus sp. [TaxId: 275]} fidphvhiylpfmatfakdthetgskaalmggtttyiemccpsrnddalegyqlwkskae gnsycdytfhmavskfdektegqlreivadgissfkiflsyknffgvddgemyqtlrlak elgvivtahcenaelvgrlqqkllsegktgpewhepsrpeaveaegtarfatflettgat gyvvhlsckpaldaamaakargvpiyiesviphflldktyaerggveamkyimspplrdk rnqkvlwdalaqgfidtvgtdhcpfdteqkllgkeaftaipngipaiedrvnllytygvs rgrldihrfvdaastkaaklfglfprkgtiavgsd
Timeline for d1gkqc2: