› 5sw5

X-ray diffraction
2.05Å resolution

Crystal structure of native catalase-peroxidase KatG at pH7.5

Released:
DOI: 10.2210/pdb5sw5/pdb
PDB entry 5sw5 coloured by chain, front view.
PDB entry 5sw5 coloured by chain, side view.
PDB entry 5sw5 coloured by chain, top view.
Source organism: Burkholderia pseudomallei 1710b
Primary publication:
A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases.
Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC
EMBO Rep 6 1156-62 (2005)
PMID: 16211084

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174650 (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
5 bound ligands:
Ligand NA 2 x NA
Ligand OXY 2 x OXY
Ligand PO4 2 x PO4
Ligand MPD 3 x MPD
Ligand TRS 4 x TRS
1 modified residue:
Ligand TOX 2 x TOX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P212121
Unit cell:
a: 100.343Å b: 114.851Å c: 174.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.149 0.184
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Probing the structure and bifunctionality of catalase-peroxidase (KatG).
Smulevich et al. (2006)
3 more