› 4ner

X-ray diffraction
1.6Å resolution

Multicopper Oxidase CueO (data1)

Released:
DOI: 10.2210/pdb4ner/pdb
PDB entry 4ner coloured by chain, front view.
PDB entry 4ner coloured by chain, side view.
PDB entry 4ner coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
New insights into the catalytic active-site structure of multicopper oxidases.
Komori H, Sugiyama R, Kataoka K, Miyazaki K, Higuchi Y, Sakurai T
Acta Crystallogr D Biol Crystallogr 70 772-9 (2014)
PMID: 24598746

Function and Biology Details

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

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: 489 amino acids
Theoretical weight: 53.54 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
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

3 bound ligands:
Ligand CU 4 x CU
Ligand OH 1 x OH
Ligand O 1 x O
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 50.398Å b: 90.721Å c: 53.37Å
α: 90° β: 102.72° γ: 90°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Three-dimensional structures of laccases.
Hakulinen et al. (2015)
3 more

1 mention without citation

Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity.
Komori et al. (2016)