3fkg

X-ray diffraction
1.81Å resolution

Crystal Structure Analysis of Fungal Versatile Peroxidase from Pleurotus eryngii

Released:
Source organism: Pleurotus eryngii
Entry authors: Piontek K, Martinez AT, Choinowski T, Plattner DA

Function and Biology Details

Reaction catalysed:
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H(2)O(2) = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Versatile peroxidase VPL2 Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 34.66 KDa
Source organism: Pleurotus eryngii
Expression system: Escherichia coli
UniProt:
  • Canonical: O94753 (Residues: 31-361; Coverage: 98%)
Gene name: vpl2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P43
Unit cell:
a: 62.683Å b: 62.683Å c: 98.217Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.152 0.201
Expression system: Escherichia coli