› 2af2

Solution NMR

Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase

Released:
DOI: 10.2210/pdb2af2/pdb
PDB entry 2af2 coloured by chain, ensemble of 30 models, front view.
PDB entry 2af2 coloured by chain, ensemble of 30 models, side view.
PDB entry 2af2 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form.
Banci L, Bertini I, Cantini F, D'Amelio N, Gaggelli E
J Biol Chem 281 2333-7 (2006)
PMID: 16291742

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 domain:

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, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 15.78 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)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, sumulated annealing, restrained energy minimization
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS.
Chattopadhyay et al. (2009)
6 more

7 mentions without citation

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