› 5sx2

X-ray diffraction
2.15Å resolution

Crystal structure of the D141E mutant of B. pseudomallei KatG at pH 8.0.

Released:
DOI: 10.2210/pdb5sx2/pdb
PDB entry 5sx2 coloured by chain, front view.
PDB entry 5sx2 coloured by chain, side view.
PDB entry 5sx2 coloured by chain, top view.
Source organism: Burkholderia pseudomallei 1710b
Primary publication:
Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei.
Deemagarn T, Wiseman B, Carpena X, Ivancich A, Fita I, Loewen PC
Proteins 66 219-28 (2007)
PMID: 17063492

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: 79.58 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 4 x OXY
Ligand MPD 3 x MPD
Ligand TRS 2 x TRS
Ligand PO4 2 x PO4
1 modified residue:
Ligand TOX 2 x TOX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 100.327Å b: 114.824Å c: 174.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.142 0.18
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Thirty years of heme catalases structural biology.
Díaz et al. (2012)
1 more