› 2fxi

X-ray diffraction
1.8Å resolution

Arsenate reductase (ArsC from pI258) C10S/C15A double mutant with sulfate in its active site

Released:
DOI: 10.2210/pdb2fxi/pdb
PDB entry 2fxi coloured by chain, front view.
PDB entry 2fxi coloured by chain, side view.
PDB entry 2fxi coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family.
Roos G, Buts L, Van Belle K, Brosens E, Geerlings P, Loris R, Wyns L, Messens J
J Mol Biol 360 826-38 (2006)
PMID: 16797027

Function and Biology Details

Reaction catalysed: 
Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140882 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arsenate reductase Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 14.78 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A006 (Residues: 1-131; Coverage: 100%)
Gene name: arsC
Sequence domains: Low molecular weight phosphotyrosine protein phosphatase
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand K 1 x K
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 33.591Å b: 33.579Å c: 99.587Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.233
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Understanding the pK(a) of redox cysteines: the key role of hydrogen bonding.
Roos et al. (2013)
2 more

2 mentions without citation

Novel roles of lysines 122, 125, and 58 in functional differences between human and murine MD-2.
Vasl et al. (2009)
1 more