› 1jzw

X-ray diffraction
1.76Å resolution

Arsenate Reductase + Sodium Arsenate From E. coli

Released:
DOI: 10.2210/pdb1jzw/pdb
PDB entry 1jzw coloured by chain, front view.
PDB entry 1jzw coloured by chain, side view.
PDB entry 1jzw coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme.
Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF
Structure 9 1071-81 (2001)
PMID: 11709171

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-140297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arsenate reductase Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.84 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08692 (Residues: 1-140; Coverage: 99%)
Gene name: arsC
Sequence domains: ArsC family
Structure domains: Glutaredoxin

Ligands and Environments

3 bound ligands:
Ligand SO4 3 x SO4
Ligand SO3 1 x SO3
Ligand CS 5 x CS
1 modified residue:
Ligand CSR 1 x CSR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 86.79Å b: 86.79Å c: 116.32Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.164 0.194
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Bacterial silver resistance: molecular biology and uses and misuses of silver compounds.
Silver S. (2003)
15 more

3 mentions without citation

Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.
Newberry et al. (2005)
2 more