› 1mng

X-ray diffraction
1.8Å resolution

STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS

Released:
DOI: 10.2210/pdb1mng/pdb
PDB entry 1mng coloured by chain, front view.
PDB entry 1mng coloured by chain, side view.
PDB entry 1mng coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus.
Lah MS, Dixon MM, Pattridge KA, Stallings WC, Fee JA, Ludwig ML
Biochemistry 34 1646-60 (1995)
PMID: 7849024

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-158269 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn] Chains: A, B
Molecule details ›
Chains: A, B
Length: 203 amino acids
Theoretical weight: 23.13 KDa
Source organism: Thermus thermophilus
Expression system: Not provided
UniProt:
  • Canonical: P61503 (Residues: 2-204; Coverage: 100%)
Gene names: TTHA0557, sodA
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 146.8Å b: 146.8Å c: 55.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Not provided

Quick links

Citations

11 review citations

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

8 mentions without citation

A Review of the Catalytic Mechanism of Human Manganese Superoxide Dismutase.
Azadmanesh et al. (2018)
7 more