› 4aul

X-ray diffraction
1.5Å resolution

Crystal structure, recombinant expression and mutagenesis studies of the bifunctional catalase-phenol oxidase from Scytalidium thermophilum

Released:
DOI: 10.2210/pdb4aul/pdb
PDB entry 4aul coloured by chain, front view.
PDB entry 4aul coloured by chain, side view.
PDB entry 4aul coloured by chain, top view.
Source organism: Mycothermus thermophilus
Primary publication:
Structure, recombinant expression and mutagenesis studies of the catalase with oxidase activity from Scytalidium thermophilum.
Yuzugullu Y, Trinh CH, Smith MA, Pearson AR, Phillips SE, Sutay Kocabas D, Bakir U, Ogel ZB, McPherson MJ
Acta Crystallogr D Biol Crystallogr 69 398-408 (2013)
PMID: 23519415

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 719 amino acids
Theoretical weight: 79.26 KDa
Source organism: Mycothermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: M4GGR6 (Residues: 1-699; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
Ligand CA 12 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 200.958Å b: 121.919Å c: 124.919Å
α: 90° β: 115.28° γ: 90°
R-values:
R R work R free
0.145 0.143 0.193
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Monofunctional Heme-Catalases.
Hansberg W. (2022)
3 other articles