5abo

X-ray diffraction
1.1Å resolution

CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-br. MUTATED RESIDUES T2K, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R, A309K AND A314R.

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
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: 35.03 KDa
Source organism: Pleurotus eryngii
Expression system: Escherichia coli str. K-12 substr. W3110
UniProt:
  • Canonical: O94753 (Residues: 33-361; Coverage: 97%)
Gene name: vpl2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 54.82Å b: 64.22Å c: 95.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.134 0.144
Expression system: Escherichia coli str. K-12 substr. W3110