› 6a6q

X-ray diffraction
1.67Å resolution

Crystal structure of a lignin peroxidase isozyme H8 variant that is stable at very acidic pH

Released:
DOI: 10.2210/pdb6a6q/pdb
PDB entry 6a6q coloured by chain, front view.
PDB entry 6a6q coloured by chain, side view.
PDB entry 6a6q coloured by chain, top view.
Source organism: Phanerochaete chrysosporium RP-78
Primary publication:
In silico-designed lignin peroxidase from Phanerochaete chrysosporium shows enhanced acid stability for depolymerization of lignin.
Pham LTM, Seo H, Kim KJ, Kim YH
Biotechnol Biofuels 11 325 (2018)
PMID: 30555531

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138895 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ligninase H8 Chain: A
Molecule details ›
Chain: A
Length: 351 amino acids
Theoretical weight: 37.67 KDa
Source organism: Phanerochaete chrysosporium RP-78
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06181 (Residues: 22-372; Coverage: 100%)
Gene name: LPOA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEB 1 x HEB
2 bound ligands:
Ligand CA 2 x CA
Ligand GOL 3 x GOL
1 modified residue:
Ligand HTR 1 x HTR

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P21
Unit cell:
a: 41.212Å b: 99.621Å c: 48.322Å
α: 90° β: 113.86° γ: 90°
R-values:
R R work R free
0.143 0.142 0.171
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

An overview of biomass conversion: exploring new opportunities.
Fülöp et al. (2020)
1 more

2 mentions without citation

Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.
Rovaletti et al. (2023)
1 more