› 2iqf

X-ray diffraction
1.86Å resolution

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-160209 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chains: A, B
Molecule details ›
Chains: A, B
Length: 505 amino acids
Theoretical weight: 58.79 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: P77872 (Residues: 1-505; Coverage: 100%)
Gene names: HP_0875, katA
Sequence domains:
Structure domains: Catalase core domain

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:
Ligand ACT 1 x ACT
Ligand O 2 x O
1 modified residue:
Ligand MHO 8 x MHO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 64.385Å b: 154.286Å c: 95.808Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.148 0.188
Expression system: Escherichia coli

Quick links

Citations

8 review citations

QM/MM methods for biomolecular systems.
Senn et al. (2009)
7 more

2 mentions without citation

QM/MM molecular dynamics studies of metal binding proteins.
Vidossich et al. (2014)
1 more