› 5kq0

X-ray diffraction
1.8Å resolution

Crystal structure of the A290D variant of catalase-peroxidase from B. pseudomallei

Released:
DOI: 10.2210/pdb5kq0/pdb
PDB entry 5kq0 coloured by chain, front view.
PDB entry 5kq0 coloured by chain, side view.
PDB entry 5kq0 coloured by chain, top view.
Source organism: Burkholderia pseudomallei 1710b
Primary publication:
The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.
Machuqueiro M, Victor B, Switala J, Villanueva J, Rovira C, Fita I, Loewen PC
Biochemistry 56 2271-2281 (2017)
PMID: 28409923

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: 79.61 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 CL 2 x CL
Ligand OXY 2 x OXY
Ligand PO4 2 x PO4
Ligand MPD 4 x MPD
1 modified residue:
Ligand TOX 2 x TOX

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 100.76Å b: 113.49Å c: 174.513Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.185
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

AQP3-mediated H2 O2 uptake inhibits LUAD autophagy by inactivating PTEN.
Wang et al. (2021)
1 more