› 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 entry 4d87 coloured by chain, front view.
PDB entry 4d87 coloured by chain, side view.
PDB entry 4d87 coloured by chain, top view.
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 97 1953-61 (2013)
PMID: 22539021

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

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109771 (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: 35.28 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

3 review citations

Diverse immune functions of hemocyanins.
Coates et al. (2014)
2 more

1 mention without citation

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