PDBe 3gtv

X-ray diffraction
2.2Å resolution

Human-mouse SOD1 chimera

Released:
Source organisms:
Primary publication:
Structures of mouse SOD1 and human/mouse SOD1 chimeras.
Arch. Biochem. Biophys. 503 183-90 (2010)
PMID: 20727846

Function and Biology Details

Reaction catalysed:
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 153 amino acids
Theoretical weight: 15.91 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P00441 (Residues: 2-90; Coverage: 58%)
  • Canonical: P08228 (Residues: 91-154; Coverage: 42%)
  • nullnull
Gene names: SOD1, Sod1
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 112.625Å b: 144.007Å c: 112.613Å
α: 90° β: 119.82° γ: 90°
R-values:
R R work R free
0.186 0.184 0.231
Expression system: Escherichia coli