› 5oc0

X-ray diffraction
1.97Å resolution

Structure of E. coli superoxide oxidase

Released:
DOI: 10.2210/pdb5oc0/pdb
PDB entry 5oc0 coloured by chain, front view.
PDB entry 5oc0 coloured by chain, side view.
PDB entry 5oc0 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Scavenging of superoxide by a membrane-bound superoxide oxidase.
Lundgren CAK, Sjöstrand D, Biner O, Bennett M, Rudling A, Johansson AL, Brzezinski P, Carlsson J, von Ballmoos C, Högbom M
Nat Chem Biol 14 788-793 (2018)
PMID: 29915379

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142045 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide oxidase CybB Chain: A
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 22.36 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABE5 (Residues: 1-176; Coverage: 100%)
Gene names: JW5224, b1418, cybB
Sequence domains: Prokaryotic cytochrome b561

Ligands and Environments

4 bound ligands:
Ligand HEM 2 x HEM
Ligand MG 1 x MG
Ligand GOL 1 x GOL
Ligand 37X 1 x 37X
1 modified residue:
Ligand MSE 11 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 68.046Å b: 91.102Å c: 97.923Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.204
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Ferric iron reductases and their contribution to unicellular ferrous iron uptake.
Cain et al. (2021)
9 more

5 mentions without citation

Scavenging of superoxide by a membrane-bound superoxide oxidase.
Lundgren et al. (2018)
4 more