› 1ahu

X-ray diffraction
2.7Å resolution

STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH P-CRESOL

Released:
DOI: 10.2210/pdb1ahu/pdb
PDB entry 1ahu coloured by chain, front view.
PDB entry 1ahu coloured by chain, side view.
PDB entry 1ahu coloured by chain, top view.
Source organism: Penicillium simplicissimum
Primary publication:
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ
Structure 5 907-20 (1997)
PMID: 9261083

Function and Biology Details

Reaction catalysed: 
Vanillyl alcohol + O(2) = vanillin + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vanillyl-alcohol oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 560 amino acids
Theoretical weight: 63.11 KDa
Source organism: Penicillium simplicissimum
UniProt:
  • Canonical: P56216 (Residues: 1-560; Coverage: 100%)
Gene name: VAOA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAA 2 x FAA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: I4
Unit cell:
a: 128.82Å b: 128.82Å c: 130.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.221 0.29

Quick links

Citations

19 review citations

Investigation of intact protein complexes by mass spectrometry.
Heck et al. (2004)
18 more

2 mentions without citation

A contact energy function considering residue hydrophobic environment and its application in protein fold recognition.
Duan et al. (2005)
1 more