› 2bkb

X-ray diffraction
1.7Å resolution

Function and Biology Details

Reaction catalysed: 
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142805 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Fe] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 192 amino acids
Theoretical weight: 21.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGD3 (Residues: 2-193; Coverage: 100%)
Gene names: JW1648, b1656, sodB
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand FE2 4 x FE2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 43.5Å b: 107.7Å c: 84.2Å
α: 90° β: 95.02° γ: 90°
R-values:
R R work R free
0.207 0.207 0.231
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

2 mentions without citation

15N-NMR characterization of His residues in and around the active site of FeSOD.
Miller et al. (2010)
1 more