› 1ye9

X-ray diffraction
2.8Å resolution

Crystal structure of proteolytically truncated catalase HPII from E. coli

Released:
DOI: 10.2210/pdb1ye9/pdb
PDB entry 1ye9 coloured by chain, front view.
PDB entry 1ye9 coloured by chain, side view.
PDB entry 1ye9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Characterization of a large subunit catalase truncated by proteolytic cleavage.
Chelikani P, Carpena X, Perez-Luque R, Donald LJ, Duckworth HW, Switala J, Fita I, Loewen PC
Biochemistry 44 5597-605 (2005)
PMID: 15823018

Function and Biology Details

Reaction catalysed: 
2 H(2)O(2) = O(2) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149123 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Catalase HPII Chains: A, B, C, D, I, J, K, L
Molecule details ›
Chains: A, B, C, D, I, J, K, L
Length: 226 amino acids
Theoretical weight: 25.62 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P21179 (Residues: 75-300; Coverage: 30%)
Gene names: JW1721, b1732, katE
Sequence domains: Catalase
Structure domains:
Catalase HPII Chains: E, F, G, H, M, N, O, P
Molecule details ›
Chains: E, F, G, H, M, N, O, P
Length: 259 amino acids
Theoretical weight: 30.07 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P21179 (Residues: 309-567; Coverage: 34%)
Gene names: JW1721, b1732, katE
Sequence domains:

Ligands and Environments


Cofactor: Ligand HDD 8 x HDD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 111.011Å b: 152.888Å c: 135.287Å
α: 90° β: 97.54° γ: 90°
R-values:
R R work R free
0.248 0.217 0.269
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Monofunctional Heme-Catalases.
Hansberg W. (2022)
1 more