› 1gge

X-ray diffraction
1.89Å resolution

CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, NATIVE STRUCTURE AT 1.9 A RESOLUTION.

Released:
DOI: 10.2210/pdb1gge/pdb
PDB entry 1gge coloured by chain, front view.
PDB entry 1gge coloured by chain, side view.
PDB entry 1gge coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli.
Melik-Adamyan W, Bravo J, Carpena X, Switala J, Maté MJ, Fita I, Loewen PC
Proteins 44 270-81 (2001)
PMID: 11455600

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: 84.27 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 HDD 4 x HDD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 93.04Å b: 132.34Å c: 121.2Å
α: 90° β: 109.63° γ: 90°
R-values:
R R work R free
0.163 0.163 0.202
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

4 mentions without citation

Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis.
Park et al. (2007)
3 more