SCOP 1.65: Domain d1nfgc2: 1nfg C:52-381

Lineage for d1nfgc2 (1nfg C:52-381)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 folds)

3. 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

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] (2 proteins)

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

7. Species Burkholderia pickettii [TaxId:329] [89488] (1 PDB entry)

8. Domain d1nfgc2: 1nfg C:52-381 [85637]
   Other proteins in same PDB: d1nfga1, d1nfgb1, d1nfgc1, d1nfgd1

Details for d1nfgc2

PDB Entry: 1nfg, 2.7 Å

PDB Description: Structure of D-hydantoinase

SCOP Domain Sequences for d1nfgc2:

Sequence; same for both SEQRES and ATOM records:

>d1nfgc2 c.1.9.6 (C:52-381) D-hydantoinase {Burkholderia pickettii}
ggidvhthvetvsfntqsadtfatatvaaacggtttivdfcqqdrghslaeavakwdgma
ggksaidygyhiivldptdsvieelevlpdlgitsfkvfmayrgmnmiddvtllktldka
vktgslvmvhaengdaadylrdkfvaegktapiyhalsrpprveaeataralalaeivna
piyivhvtceesleevmraksrgvralaetcthylyltkedlerpdfegakyvftppara
kkdhdvlwnalrngvfetvssdhcswlfkghkdrgrndfraipngapgveerlmmvyqgv
negrisltqfvelvatrpakvfgmfpqkgt

Timeline for d1nfgc2:

• d1nfgc2 is new in SCOP 1.65
  
• d1nfgc2 appears in SCOP 1.67
  
• d1nfgc2 appears in the current release, SCOPe 2.08