› 1b85

X-ray diffraction
1.85Å resolution

Function and Biology Details

Reaction catalysed: 
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H(2)O(2) = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138895 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ligninase H8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 37.44 KDa
Source organism: Phanerodontia chrysosporium
Expression system: Escherichia coli
UniProt:
  • Canonical: P06181 (Residues: 22-372; Coverage: 100%)
Gene name: LPOA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2221
Unit cell:
a: 73.4Å b: 94.4Å c: 230.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.142 0.181
Expression system: Escherichia coli

Quick links

Citations

13 review citations

New and classic families of secreted fungal heme peroxidases.
Hofrichter et al. (2010)
12 more

5 mentions without citation

Evolution of Protein Structure and Stability in Global Warming.
Barik S. (2020)
4 more