› 1i0h

X-ray diffraction
1.35Å resolution

CRYSTAL STRUCTURE OF THE E. COLI MANGANESE SUPEROXIDE DISMUTASE MUTANT Y174F AT 1.35 ANGSTROMS RESOLUTION.

Released:
DOI: 10.2210/pdb1i0h/pdb
PDB entry 1i0h coloured by chain, front view.
PDB entry 1i0h coloured by chain, side view.
PDB entry 1i0h coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity.
Edwards RA, Whittaker MM, Whittaker JW, Baker EN, Jameson GB
Biochemistry 40 4622-32 (2001)
PMID: 11294629

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-132509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn] Chains: A, B
Molecule details ›
Chains: A, B
Length: 205 amino acids
Theoretical weight: 22.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00448 (Residues: 2-206; Coverage: 100%)
Gene names: JW3879, b3908, sodA
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
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 46.893Å b: 46.017Å c: 95.993Å
α: 90° β: 98.4° γ: 90°
R-values:
R R work R free
0.17 0.17 0.196
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

5 mentions without citation

Inclusion of multiple fragment types in the site identification by ligand competitive saturation (SILCS) approach.
Raman et al. (2013)
4 more