1wx5

X-ray diffraction
2.02Å resolution

Crystal Structure of the copper-free Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein in the monoclinic crystal

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosinase Chains: A, C
Molecule details ›
Chains: A, C
Length: 281 amino acids
Theoretical weight: 32.09 KDa
Source organism: Streptomyces castaneoglobisporus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83WS2 (Residues: 1-273; Coverage: 100%)
Sequence domains: Common central domain of tyrosinase
Structure domains: Di-copper center containing domain from catechol oxidase
MelC Chains: B, D
Molecule details ›
Chains: B, D
Length: 134 amino acids
Theoretical weight: 14.2 KDa
Source organism: Streptomyces castaneoglobisporus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83WS1 (Residues: 1-126; Coverage: 100%)
Sequence domains: Tyrosinase co-factor MelC1
Structure domains: protein ne1242 domain like

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 58.85Å b: 93.2Å c: 65.59Å
α: 90° β: 93.8° γ: 90°
R-values:
R R work R free
0.206 0.201 0.291
Expression system: Escherichia coli