› 1zte

X-ray diffraction
1.85Å resolution

Contribution to Structure and Catalysis of Tyrosine 34 in Human Manganese Suerpoxide Dismutase

Released:
DOI: 10.2210/pdb1zte/pdb
PDB entry 1zte coloured by chain, front view.
PDB entry 1zte coloured by chain, side view.
PDB entry 1zte coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis.
Perry JJ, Hearn AS, Cabelli DE, Nick HS, Tainer JA, Silverman DN
Biochemistry 48 3417-24 (2009)
PMID: 19265433

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 198 amino acids
Theoretical weight: 22.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04179 (Residues: 25-222; Coverage: 89%)
Gene name: SOD2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 73.665Å b: 77.837Å c: 136.222Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.245
Expression system: Escherichia coli

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Citations

6 review citations

Superoxide dismutases and superoxide reductases.
Sheng et al. (2014)
5 more

3 mentions without citation

The structure-function relationships and physiological roles of MnSOD mutants.
Bonetta Valentino R. (2022)
2 more