› 5vf9

X-ray diffraction
1.82Å resolution

Native human manganese superoxide dismutase

Released:
DOI: 10.2210/pdb5vf9/pdb
PDB entry 5vf9 coloured by chain, front view.
PDB entry 5vf9 coloured by chain, side view.
PDB entry 5vf9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substrate-analog binding and electrostatic surfaces of human manganese superoxide dismutase.
Azadmanesh J, Trickel SR, Borgstahl GEO
J Struct Biol 199 68-75 (2017)
PMID: 28461152

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn], mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 199 amino acids
Theoretical weight: 22.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04179 (Residues: 24-222; Coverage: 90%)
Gene name: SOD2
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MN 2 x MN
Ligand PO4 2 x PO4
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P6122
Unit cell:
a: 78.24Å b: 78.24Å c: 238.47Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.192 0.221
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The structure-function relationships and physiological roles of MnSOD mutants.
Bonetta Valentino R. (2022)
3 other articles

8 mentions without citation

A Review of the Catalytic Mechanism of Human Manganese Superoxide Dismutase.
Azadmanesh et al. (2018)
7 more