› 1cob

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE SOLUTION AND REFINEMENT OF THE SEMISYNTHETIC COBALT SUBSTITUTED BOVINE ERYTHROCYTE ENZYME SUPEROXIDE DISMUTASE AT 2.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1cob/pdb
PDB entry 1cob coloured by chain, front view.
PDB entry 1cob coloured by chain, side view.
PDB entry 1cob coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure solution and refinement of the semisynthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0 A resolution.
Djinovic K, Coda A, Antolini L, Pelosi G, Desideri A, Falconi M, Rotilio G, Bolognesi M
J Mol Biol 226 227-38 (1992)
PMID: 1619651

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-132501 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B
Molecule details ›
Chains: A, B
Length: 151 amino acids
Theoretical weight: 15.57 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00442 (Residues: 2-152; 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 CU 2 x CU
Ligand CO 2 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 50.99Å b: 147.63Å c: 47.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 not available not available
Expression system: Not provided

Quick links

Citations

18 citation in other articles

Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein.
Lyons et al. (1996)
17 more

2 mentions without citation

Do all backbone polar groups in proteins form hydrogen bonds?
Fleming et al. (2005)
1 more