› 6iss

X-ray diffraction
1.53Å resolution

Lignin peroxidase H8 triple mutant S49C/A67C/H239

Released:
DOI: 10.2210/pdb6iss/pdb
PDB entry 6iss coloured by chain, front view.
PDB entry 6iss coloured by chain, side view.
PDB entry 6iss coloured by chain, top view.
Source organism: Phanerochaete chrysosporium RP-78
Primary publication:
Extra disulfide and ionic salt bridge improves the thermostability of lignin peroxidase H8 under acidic condition
Son H, Seo H, Han S, Kim S, Thanh L, Khan M, Sung H, Kang SH, Kim KJ, Kim Y
Enzyme Microb. Technol. 148 109803- (2021)

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 Chains: A, G
Molecule details ›
Chains: A, G
Length: 351 amino acids
Theoretical weight: 37.54 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:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand CA 4 x CA
1 modified residue:
Ligand HTR 2 x HTR

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: C2221
Unit cell:
a: 72.959Å b: 93.74Å c: 227.371Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.196
Expression system: Escherichia coli BL21(DE3)

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