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

  1. Root: SCOP 1.71
  2. 570216Class c: Alpha and beta proteins (a/b) [51349] (134 folds)
  3. 570217Fold 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. 572244Superfamily c.1.9: Metallo-dependent hydrolases [51556] (13 families) (S)
    the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
    has transition metal ions bound inside the barrel
  5. 572364Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (3 proteins)
  6. 572365Protein D-hydantoinase [75074] (3 species)
  7. 572380Species Thermus sp. [TaxId:275] [75075] (2 PDB entries)
  8. 572390Domain d1gkqd2: 1gkq D:55-389 [70250]
    Other proteins in same PDB: d1gkqa1, d1gkqb1, d1gkqc1, d1gkqd1
    complexed with kcx, zn

Details for d1gkqd2

PDB Entry: 1gkq (more details), 2.6 Å

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

SCOP Domain Sequences for d1gkqd2:

Sequence; same for both SEQRES and ATOM records: (download)

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

SCOP Domain Coordinates for d1gkqd2:

Click to download the PDB-style file with coordinates for d1gkqd2.
(The format of our PDB-style files is described here.)

Timeline for d1gkqd2: