› 1ggk

X-ray diffraction
2.26Å resolution

CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, ASN201HIS VARIANT.

Released:
DOI: 10.2210/pdb1ggk/pdb
PDB entry 1ggk coloured by chain, front view.
PDB entry 1ggk coloured by chain, side view.
PDB entry 1ggk 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: 84.3 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
Spacegroup: P21
Unit cell:
a: 95.23Å b: 134.7Å c: 124.45Å
α: 90° β: 109.41° γ: 90°
R-values:
R R work R free
0.143 0.13 0.208
Expression system: Escherichia coli

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Citations

3 review citations

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