› 3sqr

X-ray diffraction
1.67Å resolution

Crystal structure of laccase from Botrytis aclada at 1.67 A resolution

Released:
DOI: 10.2210/pdb3sqr/pdb
PDB entry 3sqr coloured by chain, front view.
PDB entry 3sqr coloured by chain, side view.
PDB entry 3sqr coloured by chain, top view.
Source organism: Botrytis aclada
Primary publication:
Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties.
Osipov E, Polyakov K, Kittl R, Shleev S, Dorovatovsky P, Tikhonova T, Hann S, Ludwig R, Popov V
Acta Crystallogr D Biol Crystallogr 70 2913-23 (2014)
PMID: 25372682

Function and Biology Details

Reaction catalysed: 
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124899 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Laccase Chain: A
Molecule details ›
Chain: A
Length: 580 amino acids
Theoretical weight: 63.67 KDa
Source organism: Botrytis aclada
Expression system: Komagataella pastoris
UniProt:
  • Canonical: H8ZRU2 (Residues: 1-580; Coverage: 100%)
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN, BMA
Carbohydrate polymer
4 bound ligands:
Ligand CU 3 x CU
Ligand NAG 5 x NAG
Ligand MAN 1 x MAN
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: KURCHATOV SNC BEAMLINE K4.4
Spacegroup: C2
Unit cell:
a: 69.67Å b: 113.5Å c: 79.91Å
α: 90° β: 108.75° γ: 90°
R-values:
R R work R free
0.166 0.165 0.191
Expression system: Komagataella pastoris

Quick links

Citations

4 review citations

Laccase engineering: from rational design to directed evolution.
Mate et al. (2015)
3 more

9 mentions without citation

Cellobiose dehydrogenase in biofuel cells.
Scheiblbrandner et al. (2022)
8 more