› 2fqe

X-ray diffraction
1.92Å resolution

Crystal Structures of E. coli Laccase CueO under different copper binding situations

Released:
DOI: 10.2210/pdb2fqe/pdb
PDB entry 2fqe coloured by chain, front view.
PDB entry 2fqe coloured by chain, side view.
PDB entry 2fqe coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of E. coli laccase CueO at different copper concentrations.
Li X, Wei Z, Zhang M, Peng X, Yu G, Teng M, Gong W
Biochem Biophys Res Commun 354 21-6 (2007)
PMID: 17217912

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multicopper oxidase CueO Chain: A
Molecule details ›
Chain: A
Length: 488 amino acids
Theoretical weight: 53.48 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P36649 (Residues: 29-516; Coverage: 100%)
Gene names: JW0119, b0123, cueO, yacK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

4 bound ligands:
Ligand CU 2 x CU
Ligand NA 1 x NA
Ligand C2O 1 x C2O
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: C2221
Unit cell:
a: 69.587Å b: 73.205Å c: 184.324Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.165 0.205
Expression system: Not provided

Quick links

Citations

37 citation in other articles

Cloning and characterization of a new laccase from Bacillus licheniformis catalyzing dimerization of phenolic acids.
Koschorreck et al. (2008)
36 more

1 mention without citation

Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins.
Lawton et al. (2009)