› 2j2m

X-ray diffraction
2.4Å resolution

Crystal Structure Analysis of Catalase from Exiguobacterium oxidotolerans

Released:
DOI: 10.2210/pdb2j2m/pdb
PDB 2j2m coloured by chain and viewed from the front.
PDB 2j2m coloured by chain and viewed from the side.
PDB 2j2m coloured by chain and viewed from the top.
Source organism: Exiguobacterium oxidotolerans
Primary publication:
Relationship between the size of the bottleneck 15 A from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates.
Hara I, Ichise N, Kojima K, Kondo H, Ohgiya S, Matsuyama H, Yumoto I
Biochemistry 46 11-22 (2007)
PMID: 17198371

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:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 491 amino acids
Theoretical weight: 56.59 KDa
Source organism: Exiguobacterium oxidotolerans
UniProt:
  • Canonical: A2A136 (Residues: 1-491; Coverage: 100%)
Gene name: ektA
Sequence domains:
Structure domains: Catalase core domain

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: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 94.267Å b: 131.935Å c: 110.642Å
α: 90° β: 107.61° γ: 90°
R-values:
R R work R free
0.201 0.199 0.23

Quick links

Citations

5 review citations

Molecular dynamics simulations: advances and applications.
Hospital et al. (2015)
4 more

3 mentions without citation

Distinctive properties of Arabidopsis SUMO paralogues support the in vivo predominant role of AtSUMO1/2 isoforms.
Castaño-Miquel et al. (2011)
2 more