› 1lga

X-ray diffraction
2.03Å resolution

CRYSTALLOGRAPHIC REFINEMENT OF LIGNIN PEROXIDASE AT 2 ANGSTROMS

Released:
DOI: 10.2210/pdb1lga/pdb
PDB entry 1lga coloured by chain, front view.
PDB entry 1lga coloured by chain, side view.
PDB entry 1lga coloured by chain, top view.
Source organism: Phanerodontia chrysosporium
Primary publication:
Crystallographic refinement of lignin peroxidase at 2 A.
Poulos TL, Edwards SL, Wariishi H, Gold MH
J Biol Chem 268 4429-40 (1993)
PMID: 8440725

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-155825 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ligninase LG2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 36.41 KDa
Source organism: Phanerodontia chrysosporium
Expression system: Not provided
UniProt:
  • Canonical: P49012 (Residues: 29-371; Coverage: 98%)
Gene names: GLG2, LIP2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:
Ligand NAG 2 x NAG
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 44.7Å b: 77.5Å c: 100Å
α: 90° β: 101° γ: 90°
R-values:
R R work R free
0.15 0.15 not available
Expression system: Not provided

Quick links

Citations

25 review citations

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

12 mentions without citation

Depolymerization and conversion of lignin to value-added bioproducts by microbial and enzymatic catalysis.
Weng et al. (2021)
11 more