› 4aue

X-ray diffraction
2.7Å resolution

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

Released:
DOI: 10.2210/pdb4aue/pdb
PDB entry 4aue coloured by chain, front view.
PDB entry 4aue coloured by chain, side view.
PDB entry 4aue 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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125990 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Catalase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 717 amino acids
Theoretical weight: 78.82 KDa
Source organism: Mycothermus thermophilus
UniProt:
  • Canonical: M4GGR5 (Residues: 1-717; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HDD 4 x HDD
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21212
Unit cell:
a: 185.447Å b: 216.342Å c: 68.607Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.251

Quick links

Citations

1 review citation

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

1 mention without citation

Purification and characterization of Terfezia claveryi TcCAT-1, a desert truffle catalase upregulated in mycorrhizal symbiosis.
Marqués-Gálvez et al. (2019)