› 1h6n

X-ray diffraction
2.11Å resolution

Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity

Released:
DOI: 10.2210/pdb1h6n/pdb
PDB entry 1h6n coloured by chain, front view.
PDB entry 1h6n coloured by chain, side view.
PDB entry 1h6n coloured by chain, top view.
Source organism: Proteus mirabilis
Primary publication:
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron.
Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM
Proteins 50 261-71 (2003)
PMID: 12486720

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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chain: A
Molecule details ›
Chain: A
Length: 484 amino acids
Theoretical weight: 55.74 KDa
Source organism: Proteus mirabilis
Expression system: Escherichia coli
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
2 bound ligands:
Ligand ACT 1 x ACT
Ligand SO4 1 x SO4
1 modified residue:
Ligand OMT 1 x OMT

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P6222
Unit cell:
a: 109.9Å b: 109.9Å c: 249.78Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.22 0.236
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The reaction mechanisms of heme catalases: an atomistic view by ab initio molecular dynamics.
Alfonso-Prieto et al. (2012)
1 more

1 mention without citation

Molecular Mechanism of Response and Adaptation of Antioxidant Enzyme System to Salt Stress in Leaves of Gymnocarpos przewalskii.
Qi et al. (2023)