› 5zrd

X-ray diffraction
2.3Å resolution

Tyrosinase from Burkholderia thailandensis (BtTYR) at low pH condition

Released:
DOI: 10.2210/pdb5zrd/pdb
PDB entry 5zrd coloured by chain, front view.
PDB entry 5zrd coloured by chain, side view.
PDB entry 5zrd coloured by chain, top view.
Source organism: Burkholderia thailandensis E264
Primary publication:
Structural Basis for Highly Efficient Production of Catechol Derivatives at Acidic pH by Tyrosinase from Burkholderia thailandensis
Son HF, Lee SH, Lee SH, Kim H, Hong H, Lee UJ, Lee PG, Kim BG, Kim KJ
ACS Catalysis 8 10375-10382 (2018)

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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174027 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosinase copper-binding domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 549 amino acids
Theoretical weight: 60.67 KDa
Source organism: Burkholderia thailandensis E264
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2T7K1 (Residues: 2-535; Coverage: 100%)
Gene name: BTH_II0649
Sequence domains: Common central domain of tyrosinase

Ligands and Environments

4 bound ligands:
Ligand CIT 4 x CIT
Ligand GOL 14 x GOL
Ligand CU 8 x CU
Ligand O 4 x O
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P3121
Unit cell:
a: 142.914Å b: 142.914Å c: 256.756Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.221
Expression system: Escherichia coli

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