› 4yvu

X-ray diffraction
2.3Å resolution

Crystal structure of CotA native enzyme in the acid condition, PH5.6

Released:
DOI: 10.2210/pdb4yvu/pdb
PDB entry 4yvu coloured by chain, front view.
PDB entry 4yvu coloured by chain, side view.
PDB entry 4yvu coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site.
Liu Z, Xie T, Zhong Q, Wang G
OpenAccess logo Acta Crystallogr F Struct Biol Commun 72 328-35 (2016)
PMID: 27050268

Function and Biology Details

Reactions catalysed: 
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O
2 bilirubin + O(2) = 2 biliverdin + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Laccase Chain: A
Molecule details ›
Chain: A
Length: 513 amino acids
Theoretical weight: 58.57 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P07788 (Residues: 1-513; Coverage: 100%)
Gene names: BSU06300, cotA, pig
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

3 bound ligands:
Ligand CU 3 x CU
Ligand EDO 4 x EDO
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P3121
Unit cell:
a: 101.73Å b: 101.73Å c: 135.572Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.159 0.187
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Laccases: structure, function, and potential application in water bioremediation.
Arregui et al. (2019)
2 more

1 mention without citation

Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site.
Liu et al. (2016)