SCOP 1.71: Domain d1ra5a2: 1ra5 A:56-375

Lineage for d1ra5a2 (1ra5 A:56-375)

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.1.9.5: Cytosine deaminase catalytic domain [69390] (1 protein)

6. Protein Cytosine deaminase catalytic domain [69391] (1 species)

7. Species Escherichia coli [TaxId:562] [69392] (8 PDB entries)

8. Domain d1ra5a2: 1ra5 A:56-375 [111760]
   Other proteins in same PDB: d1ra5a1
   complexed with fe, fpy, gol; mutant

Details for d1ra5a2

PDB Entry: 1ra5, 1.4 Å

PDB Description: Bacterial cytosine deaminase D314A mutant bound to 5-fluoro-4-(S)-hydroxyl-3,4-dihydropyrimidine.

SCOP Domain Sequences for d1ra5a2:

Sequence; same for both SEQRES and ATOM records:

>d1ra5a2 c.1.9.5 (A:56-375) Cytosine deaminase catalytic domain {Escherichia coli}
pfvephihldttqtagqpnwnqsgtlfegierwaerkallthddvkqrawqtlkwqiang
iqhvrthvdvsdatltalkamlevkqevapwidlqivafpqegilsypngealleealrl
gadvvgaiphfeftreygveslhktfalaqkydrlidvhcdeiddeqsrfvetvaalahh
egmgarvtashttamhsyngaytsrlfrllkmsginfvanplvnihlqgrfdtypkrrgi
trvkemlesginvcfghdavfdpwyplgtanmlqvlhmglhvcqlmgygqindglnlith
hsartlnlqdygiaagnsan

Timeline for d1ra5a2:

• d1ra5a2 is new in SCOP 1.71
  
• d1ra5a2 appears in SCOP 1.73
  
• d1ra5a2 appears in the current release, SCOPe 2.07