5kqk

X-ray diffraction
1.75Å resolution

Crystal structure of the Q233E/N240D variant of the catalase-peroxidase from B. pseudomallei

Released:

Function and Biology Details

Reaction catalysed:
2 H(2)O(2) = O(2) + 2 H(2)O
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase-peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 728 amino acids
Theoretical weight: 79.57 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3JNW6 (Residues: 1-728; Coverage: 100%)
Gene names: BURPS1710b_3366, katG
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 100.723Å b: 115.053Å c: 174.512Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.182
Expression system: Escherichia coli