› 1qwm

X-ray diffraction
1.6Å resolution

Structure of Helicobacter pylori catalase with formic acid bound

Released:
DOI: 10.2210/pdb1qwm/pdb
PDB entry 1qwm coloured by chain, front view.
PDB entry 1qwm coloured by chain, side view.
PDB entry 1qwm coloured by chain, top view.
Source organism: Helicobacter pylori
Primary publication:
Structure of Helicobacter pylori catalase, with and without formic acid bound, at 1.6 A resolution.
Loewen PC, Carpena X, Rovira C, Ivancich A, Perez-Luque R, Haas R, Odenbreit S, Nicholls P, Fita I
Biochemistry 43 3089-103 (2004)
PMID: 15023060

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160209 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chains: A, B
Molecule details ›
Chains: A, B
Length: 505 amino acids
Theoretical weight: 58.73 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: P77872 (Residues: 1-505; Coverage: 100%)
Gene names: HP_0875, katA
Sequence domains:
Structure domains: Catalase core domain

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:
Ligand AZI 1 x AZI
Ligand FMT 36 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 64.756Å b: 154.961Å c: 96.163Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.227
Expression system: Escherichia coli

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Citations

9 review citations

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
Mishra et al. (2012)
8 more