X-ray diffraction
3.1Å resolution

Crystal Structure of the Catalase-Peroxidase (KatG) R418L mutant from Mycobacterium Tuberculosis


Function and Biology Details

Reaction catalysed:
2 H(2)O(2) = O(2) + 2 H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Catalase-peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 740 amino acids
Theoretical weight: 80.64 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
  • Canonical: P9WIE5 (Residues: 1-740; Coverage: 100%)
Gene names: MTCY180.10, Rv1908c, katG
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments

Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P42212
Unit cell:
a: 150.69Å b: 150.69Å c: 157.12Å
α: 90° β: 90° γ: 90°
R R work R free
0.163 0.16 0.214
Expression system: Escherichia coli