› 3kw8

X-ray diffraction
2.29Å resolution

Two-domain laccase from Streptomyces coelicolor at 2.3 A resolution

Released:
DOI: 10.2210/pdb3kw8/pdb
PDB entry 3kw8 coloured by chain, front view.
PDB entry 3kw8 coloured by chain, side view.
PDB entry 3kw8 coloured by chain, top view.
Source organism: Streptomyces coelicolor
Primary publication:
Structure of laccase from Streptomyces coelicolor after soaking with potassium hexacyanoferrate and at an improved resolution of 2.3 Å.
Skálová T, Dušková J, Hašek J, Stěpánková A, Koval T, Østergaard LH, Dohnálek J
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 27-32 (2011)
PMID: 21206017

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:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-578587 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper oxidase Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 30.38 KDa
Source organism: Streptomyces coelicolor
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: Q9XAL8 (Residues: 42-317; Coverage: 81%)
Gene names: SC4C6.22, SCO6712
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

5 bound ligands:
Ligand CU 4 x CU
Ligand FE 1 x FE
Ligand NA 2 x NA
Ligand PG4 2 x PG4
Ligand PGE 3 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P4332
Unit cell:
a: 176.723Å b: 176.723Å c: 176.723Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.178
Expression system: Aspergillus oryzae

Quick links

Citations

6 citation in other articles

Direct bio-electrocatalysis of O2 reduction by Streptomyces coelicolor laccase orientated at promoter-modified graphite electrodes.
Lörcher et al. (2013)
5 more

3 mentions without citation

Functional and protective hole hopping in metalloenzymes.
Gray et al. (2021)
2 more