› 5o40

X-ray diffraction
1.5Å 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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132494 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, F
Molecule details ›
Chains: A, F
Length: 153 amino acids
Theoretical weight: 15.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00441 (Residues: 2-154; Coverage: 99%)
Gene name: SOD1
Sequence domains: Copper/zinc superoxide dismutase (SODC)

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand 9JT 2 x 9JT
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 38.1Å b: 67.84Å c: 51.04Å
α: 90° β: 106.35° γ: 90°
R-values:
R R work R free
0.171 0.168 0.215
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Antioxidants: Positive or Negative Actors?
Salehi et al. (2018)
10 more

4 mentions without citation

Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants.
Huai et al. (2019)
3 more