› 5oc1

X-ray diffraction
2.3Å resolution

Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid

Released:
DOI: 10.2210/pdb5oc1/pdb
Model geometry
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Source organism: Pleurotus eryngii
Primary publication:
Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase.
Carro J, Martínez-Júlvez M, Medina M, Martínez AT, Ferreira P
Phys Chem Chem Phys 19 28666-28675 (2017)
PMID: 29043303

Function and Biology Details

Reaction catalysed: 
An aromatic primary alcohol + O(2) = an aromatic aldehyde + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 565 amino acids
Theoretical weight: 60.93 KDa
Source organism: Pleurotus eryngii
Expression system: Escherichia coli
UniProt:
  • Canonical: O94219 (Residues: 29-593; Coverage: 99%)
Gene name: aao
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
Ligand ANN 1 x ANN
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P6422
Unit cell:
a: 179.326Å b: 179.326Å c: 160.177Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.174 0.195
Expression system: Escherichia coli

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Citations

1 review citation

Pecularities and applications of aryl-alcohol oxidases from fungi.
Urlacher et al. (2021)
5 other articles

7 mentions without citation

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.
Bissaro et al. (2018)
6 more

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