› 1isa

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/pdb1isa/pdb
PDB entry 1isa coloured by chain, front view.
PDB entry 1isa coloured by chain, side view.
PDB entry 1isa coloured by chain, top view.
Source organism: Escherichia coli
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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142805 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Fe] Chains: A, B
Molecule details ›
Chains: A, B
Length: 192 amino acids
Theoretical weight: 21.15 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0AGD3 (Residues: 2-193; Coverage: 100%)
Gene names: JW1648, b1656, sodB
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand FE2 2 x FE2
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 81.55Å b: 75.08Å c: 71.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Not provided

Quick links

Citations

12 review citations

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

20 mentions without citation

Why is manganese so valuable to bacterial pathogens?
Čapek et al. (2023)
19 more