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Solution NMR

The Solution Structure of Reduced Dimeric Copper Zinc SOD: the Structural Effects of Dimerization

Released:
DOI: 10.2210/pdb1l3n/pdb
PDB entry 1l3n coloured by chain, ensemble of 30 models, front view.
PDB entry 1l3n coloured by chain, ensemble of 30 models, side view.
PDB entry 1l3n coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization.
Banci L, Bertini I, Cramaro F, Del Conte R, Viezzoli MS
Eur J Biochem 269 1905-15 (2002)
PMID: 11952792

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

2 bound ligands:
Ligand CU1 2 x CU1
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing and restrained enegy minimization in vacuum
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The structural biochemistry of the superoxide dismutases.
Perry et al. (2010)
4 more

8 mentions without citation

The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase.
Sirangelo et al. (2017)
7 more