3f0i

X-ray diffraction
1.88Å resolution

Arsenate reductase from Vibrio cholerae.

Released:
Source organism: Vibrio cholerae
Entry authors: Osipiuk J, Gu M, Stam J, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
Arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arsenate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 119 amino acids
Theoretical weight: 13.65 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KQ39 (Residues: 2-116; Coverage: 99%)
Gene name: VC_2165
Sequence domains: ArsC family
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P6422
Unit cell:
a: 118.704Å b: 118.704Å c: 110.013Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.166 0.189
Expression system: Escherichia coli