› 1msd

X-ray diffraction
3.2Å resolution

COMPARISON OF THE CRYSTAL STRUCTURES OF GENETICALLY ENGINEERED HUMAN MANGANESE SUPEROXIDE DISMUTASE AND MANGANESE SUPEROXIDE DISMUTASE FROM THERMUS THERMOPHILUS. DIFFERENCES IN DIMER-DIMER INTERACTIONS.

Released:
DOI: 10.2210/pdb1msd/pdb
PDB entry 1msd coloured by chain, front view.
PDB entry 1msd coloured by chain, side view.
PDB entry 1msd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction.
Wagner UG, Pattridge KA, Ludwig ML, Stallings WC, Werber MM, Oefner C, Frolow F, Sussman JL
Protein Sci 2 814-25 (1993)
PMID: 8495200

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 domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn], mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 22.23 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04179 (Residues: 25-222; Coverage: 89%)
Gene name: SOD2
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 77.8Å b: 74.1Å c: 68.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 not available
Expression system: Not provided

Quick links

Citations

3 review citations

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

6 mentions without citation

Toward a resolution of the introns early/late debate: only phase zero introns are correlated with the structure of ancient proteins.
de Souza et al. (1998)
5 more