› 1k6w

X-ray diffraction
1.75Å resolution

The Structure of Escherichia coli Cytosine Deaminase

Released:
DOI: 10.2210/pdb1k6w/pdb
PDB entry 1k6w coloured by chain, front view.
PDB entry 1k6w coloured by chain, side view.
PDB entry 1k6w coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of Escherichia coli cytosine deaminase.
Ireton GC, McDermott G, Black ME, Stoddard BL
J Mol Biol 315 687-97 (2002)
PMID: 11812140

Function and Biology Details

Reaction catalysed: 
Cytosine + H(2)O = uracil + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150496 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosine deaminase Chain: A
Molecule details ›
Chain: A
Length: 426 amino acids
Theoretical weight: 47.51 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P25524 (Residues: 2-427; Coverage: 100%)
Gene names: JW0328, b0337, codA
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FE 1 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: R32
Unit cell:
a: 109.15Å b: 109.15Å c: 240.05Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.157 0.155 0.172
Expression system: Escherichia coli

Quick links

Citations

11 review citations

RNA editing by adenosine deaminases that act on RNA.
Bass BL. (2002)
10 more

8 mentions without citation

Structural bases for CRMP function in plexin-dependent semaphorin3A signaling.
Deo et al. (2004)
7 more