› 1s3d

X-ray diffraction
1.54Å resolution

ARSENATE REDUCTASE R60A MUTANT FROM E. COLI

Released:
DOI: 10.2210/pdb1s3d/pdb
PDB entry 1s3d coloured by chain, front view.
PDB entry 1s3d coloured by chain, side view.
PDB entry 1s3d coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product.
DeMel S, Shi J, Martin P, Rosen BP, Edwards BF
Protein Sci 13 2330-40 (2004)
PMID: 15295115

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 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: 138 amino acids
Theoretical weight: 15.42 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08692 (Residues: 3-140; Coverage: 98%)
Gene name: arsC
Sequence domains: ArsC family
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand CS 5 x CS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 86.6Å b: 86.6Å c: 115.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.138 not available 0.198
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Glutathione analogs in prokaryotes.
Fahey RC. (2013)
3 more

4 mentions without citation

The electronic structure of Mn in oxides, coordination complexes, and the oxygen-evolving complex of photosystem II studied by resonant inelastic X-ray scattering.
Glatzel et al. (2004)
3 more