› 4d87

X-ray diffraction
3.5Å resolution

Crystal Structure of Tyrosinase from Bacillus megaterium in complex with SDS

Released:
DOI: 10.2210/pdb4d87/pdb
PDB 4d87 coloured by chain and viewed from the front.
PDB 4d87 coloured by chain and viewed from the side.
PDB 4d87 coloured by chain and viewed from the top.
Source organism: Priestia megaterium
Primary publication:
Changes in tyrosinase specificity by ionic liquids and sodium dodecyl sulfate.
Goldfeder M, Egozy M, Shuster Ben-Yosef V, Adir N, Fishman A
Appl. Microbiol. Biotechnol. (2012)
PMID: 22539021

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
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 35.28 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
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

2 bound ligands:
Ligand CU 2 x CU
Ligand SDS 1 x SDS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 47.84Å b: 79.14Å c: 85.93Å
α: 90° β: 103.56° γ: 90°
R-values:
R R work R free
0.262 0.259 0.293
Expression system: Escherichia coli

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Citations

4 review citations

Similar but Still Different: Which Amino Acid Residues Are Responsible for Varying Activities in Type-III Copper Enzymes?
Kampatsikas et al. (2021)
3 more