› 1vzg

X-ray diffraction
1.69Å resolution

Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced photoreduction

Released:
DOI: 10.2210/pdb1vzg/pdb
PDB entry 1vzg coloured by chain, front view.
PDB entry 1vzg coloured by chain, side view.
PDB entry 1vzg coloured by chain, top view.
Source organism: Desulfarculus baarsii
Primary publication:
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.
Adam V, Royant A, Nivière V, Molina-Heredia FP, Bourgeois D
Structure 12 1729-40 (2004)
PMID: 15341736

Function and Biology Details

Reaction catalysed: 
Reduced rubredoxin + superoxide + 2 H(+) = oxidized rubredoxin + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175122 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Desulfoferrodoxin Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 14.12 KDa
Source organism: Desulfarculus baarsii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q46495 (Residues: 1-126; Coverage: 100%)
Gene names: Deba_2050, dfx, rbo
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand FE 4 x FE
Ligand CA 1 x CA
Ligand FC6 2 x FC6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 42.13Å b: 67.65Å c: 82.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.249
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin.
Kurtz DM. (2006)
2 more

2 mentions without citation

Superoxide dismutases and superoxide reductases.
Sheng et al. (2014)
1 more