› 1j9b

X-ray diffraction
1.26Å resolution

ARSENATE REDUCTASE+0.4M ARSENITE FROM E. COLI

Released:
DOI: 10.2210/pdb1j9b/pdb
PDB entry 1j9b coloured by chain, front view.
PDB entry 1j9b coloured by chain, side view.
PDB entry 1j9b 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: 141 amino acids
Theoretical weight: 15.94 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P08692 (Residues: 1-141; Coverage: 100%)
Gene name: arsC
Sequence domains: ArsC family
Structure domains: Glutaredoxin

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand CS 3 x CS
Ligand TAS 2 x TAS
1 modified residue:
Ligand CZZ 1 x CZZ

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6122
Unit cell:
a: 86.613Å b: 86.613Å c: 116.672Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.14 0.134 0.175

Quick links

Citations

17 review citations

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

4 mentions without citation

Global mapping of the protein structure space and application in structure-based inference of protein function.
Hou et al. (2005)
3 more