› 1luw

X-ray diffraction
2.3Å resolution

CATALYTIC AND STRUCTURAL EFFECTS OF AMINO-ACID SUBSTITUTION AT HIS 30 IN HUMAN MANGANESE SUPEROXIDE DISMUTASE: INSERTION OF VAL CGAMMA INTO THE SUBSTRATE ACCESS CHANNEL

Released:
DOI: 10.2210/pdb1luw/pdb
PDB entry 1luw coloured by chain, front view.
PDB entry 1luw coloured by chain, side view.
PDB entry 1luw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel.
Hearn AS, Stroupe ME, Cabelli DE, Ramilo CA, Luba JP, Tainer JA, Nick HS, Silverman DN
Biochemistry 42 2781-9 (2003)
PMID: 12627943

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: 22.22 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

2 bound ligands:
Ligand MN 2 x MN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P6122
Unit cell:
a: 79.364Å b: 79.364Å c: 242.576Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.239 0.282
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

3 mentions without citation

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