SCOPe 2.05: Domain d1nfgb2: 1nfg B:52-381

Lineage for d1nfgb2 (1nfg B:52-381)

1. Root: SCOPe 2.05

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 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] (19 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] (5 proteins)
   automatically mapped to Pfam PF13147

6. Protein D-hydantoinase [75074] (4 species)

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

8. Domain d1nfgb2: 1nfg B:52-381 [85635]
   Other proteins in same PDB: d1nfga1, d1nfgb1, d1nfgc1, d1nfgd1
   complexed with zn

Details for d1nfgb2

PDB Entry: 1nfg, 2.7 Å

PDB Description: Structure of D-hydantoinase

PDB Compounds: (B:) D-hydantoinase

SCOPe Domain Sequences for d1nfgb2:

Sequence; same for both SEQRES and ATOM records:

>d1nfgb2 c.1.9.6 (B:52-381) D-hydantoinase {Burkholderia pickettii [TaxId: 329]}
ggidvhthvetvsfntqsadtfatatvaaacggtttivdfcqqdrghslaeavakwdgma
ggksaidygyhiivldptdsvieelevlpdlgitsfkvfmayrgmnmiddvtllktldka
vktgslvmvhaengdaadylrdkfvaegktapiyhalsrpprveaeataralalaeivna
piyivhvtceesleevmraksrgvralaetcthylyltkedlerpdfegakyvftppara
kkdhdvlwnalrngvfetvssdhcswlfkghkdrgrndfraipngapgveerlmmvyqgv
negrisltqfvelvatrpakvfgmfpqkgt

Timeline for d1nfgb2:

• d1nfgb2 first appeared in SCOP 1.65
  
• d1nfgb2 appears in SCOPe 2.04
  
• d1nfgb2 appears in SCOPe 2.06
  
• d1nfgb2 appears in the current release, SCOPe 2.08