› 1cf9

X-ray diffraction
1.8Å resolution

Structure of the mutant VAL169CYS of catalase HPII from Escherichia coli

Released:
DOI: 10.2210/pdb1cf9/pdb
PDB entry 1cf9 coloured by chain, front view.
PDB entry 1cf9 coloured by chain, side view.
PDB entry 1cf9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.
Maté MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I
J Biol Chem 274 27717-25 (1999)
PMID: 10488114

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 domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149122 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase HPII Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 753 amino acids
Theoretical weight: 84.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P21179 (Residues: 1-753; Coverage: 100%)
Gene names: JW1721, b1732, katE
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 93.47Å b: 133.04Å c: 122.22Å
α: 90° β: 109.64° γ: 90°
R-values:
R R work R free
0.181 0.181 0.237
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Evolution of catalases from bacteria to humans.
Zamocky et al. (2008)
1 more

1 mention without citation

Investigation of the Importance of Protein 3D Structure for Assessing Conservation of Lysine Acetylation Sites in Protein Homologs.
Jew et al. (2021)