› 4qoq

X-ray diffraction
1.7Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
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: 56.78 KDa
Source organism: Bacillus pumilus
Expression system: Escherichia coli
Structure domains: Catalase core domain

Ligands and Environments

4 bound ligands:
Ligand HEM 8 x HEM
Ligand JZ3 6 x JZ3
Ligand CL 6 x CL
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 91.79Å b: 108.109Å c: 103.409Å
α: 90° β: 91.98° γ: 90°
R-values:
R R work R free
0.163 0.162 0.19
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin.
Petrik et al. (2016)
6 more

1 mention without citation

Monofunctional Heme-Catalases.
Hansberg W. (2022)