4fcs

X-ray diffraction
1.5Å resolution

The crystal structures of several mutants of pleurotus eryngii versatile peroxidase

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: 315 amino acids
Theoretical weight: 33.15 KDa
Source organism: Pleurotus eryngii
Expression system: Escherichia coli
UniProt:
  • Canonical: O94753 (Residues: 31-345; Coverage: 93%)
Gene name: vpl2
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I41
Unit cell:
a: 96.271Å b: 96.271Å c: 98.907Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.15 0.176
Expression system: Escherichia coli