SCOP 1.65: Domain d1nfgd2: 1nfg D:52-381

Lineage for d1nfgd2 (1nfg D: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 d1nfgd2: 1nfg D:52-381 [85639]
   Other proteins in same PDB: d1nfga1, d1nfgb1, d1nfgc1, d1nfgd1
   complexed with kcx, zn

Details for d1nfgd2

PDB Entry: 1nfg, 2.7 Å

PDB Description: Structure of D-hydantoinase

SCOP Domain Sequences for d1nfgd2:

Sequence; same for both SEQRES and ATOM records:

>d1nfgd2 c.1.9.6 (D:52-381) D-hydantoinase {Burkholderia pickettii}
ggidvhthvetvsfntqsadtfatatvaaacggtttivdfcqqdrghslaeavakwdgma
ggksaidygyhiivldptdsvieelevlpdlgitsfkvfmayrgmnmiddvtllktldka
vktgslvmvhaengdaadylrdkfvaegktapiyhalsrpprveaeataralalaeivna
piyivhvtceesleevmraksrgvralaetcthylyltkedlerpdfegakyvftppara
kkdhdvlwnalrngvfetvssdhcswlfkghkdrgrndfraipngapgveerlmmvyqgv
negrisltqfvelvatrpakvfgmfpqkgt

Timeline for d1nfgd2:

• d1nfgd2 is new in SCOP 1.65
  
• d1nfgd2 appears in SCOP 1.67
  
• d1nfgd2 appears in the current release, SCOPe 2.08