4hd4

X-ray diffraction
1.8Å resolution

Crystal Structure of Tyrosinase from Bacillus megaterium V218F mutant

Released:
Source organism: Priestia megaterium
Primary publication:
Influencing the monophenolase/diphenolase activity ratio in tyrosinase.
Biochim Biophys Acta 1834 629-33 (2013)
PMID: 23305929

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-502569 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosinase copper-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 35.3 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • 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: 48Å b: 78.58Å c: 85.89Å
α: 90° β: 106.13° γ: 90°
R-values:
R R work R free
0.209 0.207 0.228
Expression system: Escherichia coli BL21(DE3)