SCOP 1.71: Domain d1k1da2: 1k1d A:53-384

Lineage for d1k1da2 (1k1d A:53-384)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold 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. 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

5. Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (3 proteins)

6. Protein D-hydantoinase [75074] (3 species)

7. Species Bacillus stearothermophilus [TaxId:1422] [75076] (1 PDB entry)

8. Domain d1k1da2: 1k1d A:53-384 [71980]
   Other proteins in same PDB: d1k1da1, d1k1db1, d1k1dc1, d1k1dd1, d1k1de1, d1k1df1, d1k1dg1, d1k1dh1

Details for d1k1da2

PDB Entry: 1k1d, 3.01 Å

PDB Description: Crystal structure of D-hydantoinase

SCOP Domain Sequences for d1k1da2:

Sequence; same for both SEQRES and ATOM records:

>d1k1da2 c.1.9.6 (A:53-384) D-hydantoinase {Bacillus stearothermophilus}
ggidphthldmplggtvtkddfesgtiaaafggtttiidfcltnkgeplkkaietwhnka
ngkavidygfhlmiseitddvleelpkvleeegitslkvfmayknvfqaddgtlyctlla
akelgalvmvhaengdvidyltkkaladgntdpiyhaltrppelegeatgracqltelag
sqlyvvhvtcaqavekiaearnkgldvwgetcpqylvldqsylekpnfegakyvwspplr
ekwhqevlwnalkngqlqtlgsdqcsfdfkgqkelgrgdftkipnggpiiedrvsilfse
gvkkgritlnqfvdivstriaklfglfpkkgt

Timeline for d1k1da2:

• d1k1da2 first appeared in SCOP 1.61
  
• d1k1da2 appears in SCOP 1.69
  
• d1k1da2 appears in SCOP 1.73
  
• d1k1da2 appears in the current release, SCOPe 2.08