› 4akp

X-ray diffraction
2Å resolution

Mutations in the neighbourhood of CotA-laccase trinuclear site: E498T mutant

Released:
DOI: 10.2210/pdb4akp/pdb
PDB entry 4akp coloured by chain, front view.
PDB entry 4akp coloured by chain, side view.
PDB entry 4akp coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis.
Chen Z, Durão P, Silva CS, Pereira MM, Todorovic S, Hildebrandt P, Bento I, Lindley PF, Martins LO
Dalton Trans 39 2875-82 (2010)
PMID: 20200715

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: 58.56 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 OXY 1 x OXY
Ligand EDO 12 x EDO
1 modified residue:
Ligand CSX 1 x CSX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3121
Unit cell:
a: 101.898Å b: 101.898Å c: 136.931Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.215
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Copper active sites in biology.
Solomon et al. (2014)
7 more

1 mention without citation

Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development.
Naumann et al. (2022)