X-ray diffraction
1.9Å resolution

Crystal Structure of Tyrosinase from Bacillus megaterium N205D mutant

Source organism: Priestia megaterium
Primary publication:
The mechanism of copper uptake by tyrosinase from Bacillus megaterium.
J Biol Inorg Chem 18 895-903 (2013)
PMID: 24061559

Function and Biology Details

Reaction catalysed:
(1a) L-tyrosine + 1/2 O(2) = L-dopa
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Tyrosinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 35.26 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21(DE3)
  • Canonical: B2ZB02 (Residues: 1-297; Coverage: 100%)
Sequence domains: Common central domain of tyrosinase
Structure domains: Di-copper center containing domain from catechol oxidase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 54.9Å b: 78.33Å c: 82.16Å
α: 90° β: 105.5° γ: 90°
R R work R free
0.194 0.193 0.21
Expression system: Escherichia coli BL21(DE3)