› 1ues

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reaction catalysed: 
2 superoxide + 2 H(+) = O(2) + 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-148683 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn/Fe] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 191 amino acids
Theoretical weight: 21.57 KDa
Source organism: Porphyromonas gingivalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P19665 (Residues: 1-191; Coverage: 100%)
Gene names: PG_1545, sod, sodB
Sequence domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL24XU
Spacegroup: P212121
Unit cell:
a: 71.68Å b: 95.12Å c: 98.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.25
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

A charge polarization model for the metal-specific activity of superoxide dismutases.
Barwinska-Sendra et al. (2018)