› 2ji2

X-ray diffraction
1.7Å resolution

X-ray structure of E114A mutant of superoxide reductase from Desulfoarculus baarsii in the native, reduced form

Released:
DOI: 10.2210/pdb2ji2/pdb
PDB entry 2ji2 coloured by chain, front view.
PDB entry 2ji2 coloured by chain, side view.
PDB entry 2ji2 coloured by chain, top view.
Source organism: Desulfarculus baarsii
Primary publication:
Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.
Katona G, Carpentier P, Nivière V, Amara P, Adam V, Ohana J, Tsanov N, Bourgeois D
Science 316 449-53 (2007)
PMID: 17446401

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 126 amino acids
Theoretical weight: 14.12 KDa
Source organism: Desulfarculus baarsii
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: Q46495 (Residues: 1-126; Coverage: 100%)
Gene names: Deba_2050, dfx, rbo
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand FE 4 x FE
Ligand NO3 4 x NO3
Ligand FE2 4 x FE2
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I222
Unit cell:
a: 70.47Å b: 82.87Å c: 201.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.222
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

7 review citations

Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent developments in enzymology and modeling studies.
Bruijnincx et al. (2008)
6 more

2 mentions without citation

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