› 3gtv

X-ray diffraction
2.2Å resolution

Human-mouse SOD1 chimera

Released:
DOI: 10.2210/pdb3gtv/pdb
PDB entry 3gtv coloured by chain, front view.
PDB entry 3gtv coloured by chain, side view.
PDB entry 3gtv coloured by chain, top view.
Source organisms:
Primary publication:
Structures of mouse SOD1 and human/mouse SOD1 chimeras.
Seetharaman SV, Taylor AB, Holloway S, Hart PJ
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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132489 (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%)
Gene names: SOD1, Sod1
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

1 bound ligand:
Ligand ZN 12 x ZN
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

Quick links

Citations

4 review citations

Transgenic and physiological mouse models give insights into different aspects of amyotrophic lateral sclerosis.
De Giorgio et al. (2019)
3 more

3 mentions without citation

Mechanisms of SOD1 regulation by post-translational modifications.
Banks et al. (2019)
2 more