5fne

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII TRIPLE MUTANT E37K, H39R & G330R

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-131734 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Versatile peroxidase VPL2 Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 34.72 KDa
Source organism: Pleurotus eryngii
Expression system: Escherichia coli str. K-12 substr. W3110
UniProt:
  • Canonical: O94753 (Residues: 31-361; Coverage: 98%)
Gene name: vpl2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21212
Unit cell:
a: 55.19Å b: 104.2Å c: 76.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.229
Expression system: Escherichia coli str. K-12 substr. W3110