Function and Biology Details
Reaction catalysed:
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Superoxide dismutase, copper/zinc binding domain
- Superoxide dismutase-like, copper/zinc binding domain superfamily
- Heavy metal-associated domain, HMA
- Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone
- Heavy metal-associated domain superfamily
- Superoxide dismutase, copper/zinc, binding site
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132492 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Superoxide dismutase [Cu-Zn]
Molecule details ›
Chains: A, C
Length: 153 amino acids
Theoretical weight: 15.84 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Length: 153 amino acids
Theoretical weight: 15.84 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
- Canonical:
P00441 (Residues: 2-154; Coverage: 99%)
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Superoxide dismutase 1 copper chaperone
Molecule details ›
Chains: B, D
Length: 248 amino acids
Theoretical weight: 27.03 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Heavy-metal-associated domain
Length: 248 amino acids
Theoretical weight: 27.03 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P40202 (Residues: 2-249; Coverage: 100%)
Sequence domains: Heavy-metal-associated domain
