Lineage for d1raka2 (1rak A:56-375)

  1. Root: SCOPe 2.06
  2. 2089713Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2089714Fold 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. 2096081Superfamily c.1.9: Metallo-dependent hydrolases [51556] (19 families) (S)
    the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
    has transition metal ions bound inside the barrel
  5. 2096351Family c.1.9.5: Cytosine deaminase catalytic domain [69390] (1 protein)
    automatically mapped to Pfam PF13147
    automatically mapped to Pfam PF07969
  6. 2096352Protein Cytosine deaminase catalytic domain [69391] (1 species)
  7. 2096353Species Escherichia coli [TaxId:562] [69392] (8 PDB entries)
    Uniprot P25524
  8. 2096356Domain d1raka2: 1rak A:56-375 [111762]
    Other proteins in same PDB: d1raka1
    complexed with fe, fpy, gol; mutant

Details for d1raka2

PDB Entry: 1rak (more details), 1.32 Å

PDB Description: Bacterial cytosine deaminase D314S mutant bound to 5-fluoro-4-(S)-hydroxyl-3,4-dihydropyrimidine.
PDB Compounds: (A:) Cytosine deaminase

SCOPe Domain Sequences for d1raka2:

Sequence; same for both SEQRES and ATOM records: (download)

>d1raka2 c.1.9.5 (A:56-375) Cytosine deaminase catalytic domain {Escherichia coli [TaxId: 562]}

SCOPe Domain Coordinates for d1raka2:

Click to download the PDB-style file with coordinates for d1raka2.
(The format of our PDB-style files is described here.)

Timeline for d1raka2:

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