› 4p6s

X-ray diffraction
2.2Å resolution

Crystal Structure of tyrosinase from Bacillus megaterium with L-DOPA in the active site

Released:
DOI: 10.2210/pdb4p6s/pdb
PDB entry 4p6s coloured by chain, front view.
PDB entry 4p6s coloured by chain, side view.
PDB entry 4p6s coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins.
Goldfeder M, Kanteev M, Isaschar-Ovdat S, Adir N, Fishman A
Nat Commun 5 4505 (2014)
PMID: 25074014

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109772 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosinase copper-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 33.29 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B2ZB02 (Residues: 4-290; Coverage: 97%)
Sequence domains: Common central domain of tyrosinase
Structure domains: Di-copper center containing domain from catechol oxidase

Ligands and Environments

2 bound ligands:
Ligand ZN 6 x ZN
Ligand DAH 4 x DAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 78.88Å b: 81.55Å c: 84.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Activation of dioxygen by copper metalloproteins and insights from model complexes.
Quist et al. (2017)
10 more

9 mentions without citation

Structure-function correlations in tyrosinases.
Kanteev et al. (2015)
8 more