› 2x87

X-ray diffraction
2Å resolution

Crystal Structure of the reconstituted CotA

Released:
DOI: 10.2210/pdb2x87/pdb
PDB entry 2x87 coloured by chain, front view.
PDB entry 2x87 coloured by chain, side view.
PDB entry 2x87 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer.
Bento I, Silva CS, Chen Z, Martins LO, Lindley PF, Soares CM
BMC Struct Biol 10 28 (2010)
PMID: 20822511

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: 58.59 KDa
Source organism: Bacillus subtilis
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 4 x CU
Ligand OH 1 x OH
Ligand EDO 7 x EDO
1 modified residue:
Ligand CSX 1 x CSX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P3121
Unit cell:
a: 101.3Å b: 101.3Å c: 136.092Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.171 0.198
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Pathways for degradation of lignin in bacteria and fungi.
Bugg et al. (2011)
7 more

3 mentions without citation

Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer.
Bento et al. (2010)
2 more