Lineage for Protein: L-hydantoinase
- Root: SCOP 1.67
Class c: Alpha and beta proteins (a/b) [51349] (130 folds) Fold c.1: TIM beta/alpha-barrel [51350] (28 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] (13 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] (3 proteins) 
Protein L-hydantoinase [75077] (1 species)
Species:
Arthrobacter aurescens [TaxId:43663] [75078] (1 PDB entry) - Domains for 1gkr:
Domain d1gkra2: 1gkr A:55-379 [70252]
Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
Domain d1gkrb2: 1gkr B:55-379 [70254]
Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
Domain d1gkrc2: 1gkr C:55-379 [70256]
Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
Domain d1gkrd2: 1gkr D:55-379 [70258]
Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
complexed with kcx, zn
- Domains for 1gkr:
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 SCOP 1.69
- Protein L-hydantoinase from c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain appears in the current release, SCOPe 2.08