› 1nm0

X-ray diffraction
2.3Å resolution

Proteus mirabilis catalase in complex with formiate

Released:
DOI: 10.2210/pdb1nm0/pdb
PDB entry 1nm0 coloured by chain, front view.
PDB entry 1nm0 coloured by chain, side view.
PDB entry 1nm0 coloured by chain, top view.
Source organism: Proteus mirabilis
Primary publication:
Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid.
Andreoletti P, Pernoud A, Sainz G, Gouet P, Jouve HM
Acta Crystallogr D Biol Crystallogr 59 2163-8 (2003)
PMID: 14646074

Function and Biology Details

Reaction catalysed: 
2 H(2)O(2) = O(2) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-154607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chain: A
Molecule details ›
Chain: A
Length: 484 amino acids
Theoretical weight: 55.73 KDa
Source organism: Proteus mirabilis
UniProt:
  • Canonical: P42321 (Residues: 1-484; Coverage: 100%)
Gene name: katA
Sequence domains:
Structure domains: Catalase core domain

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
3 bound ligands:
Ligand SO4 6 x SO4
Ligand FMT 1 x FMT
Ligand GOL 1 x GOL
1 modified residue:
Ligand OMT 1 x OMT

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P6222
Unit cell:
a: 110Å b: 110Å c: 250Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.211

Quick links

Citations

3 review citations

Classical catalase: ancient and modern.
Nicholls P. (2012)
2 more