SCOP 1.63: Protein: L-hydantoinase

Lineage for Protein: L-hydantoinase

Root: SCOP 1.63
Class c: Alpha and beta proteins (a/b) [51349] (117 folds)

Fold c.1: TIM beta/alpha-barrel [51350] (26 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] (12 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] (2 proteins)
Protein L-hydantoinase [75077] (1 species)

Species:

Arthrobacter aurescens [TaxId:43663] [75078] (1 PDB entry)
- Domains for 1gkr:
  1. Domain d1gkra2: 1gkr A:55-379 [70252]
    Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
  2. Domain d1gkrb2: 1gkr B:55-379 [70254]
    Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
  3. Domain d1gkrc2: 1gkr C:55-379 [70256]
    Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
  4. Domain d1gkrd2: 1gkr D:55-379 [70258]
    Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
    complexed with kcx, zn

More info for Protein L-hydantoinase from c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain

Timeline for Protein L-hydantoinase from c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain:

Protein L-hydantoinase from c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain first appeared in SCOP 1.61
Protein L-hydantoinase from c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain appears in SCOP 1.65
Protein L-hydantoinase from c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain appears in the current release, SCOPe 2.08