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› 6ju6

X-ray diffraction
1.5Å resolution

Aspergillus oryzae active-tyrosinase copper-depleted C92A mutant

Released:
DOI: 10.2210/pdb6ju6/pdb
Model geometry
Fit model/data
PDB entry 6ju6 coloured by chain, front view.
PDB entry 6ju6 coloured by chain, side view.
PDB entry 6ju6 coloured by chain, top view.
Source organism: Aspergillus oryzae
Primary publication:
Copper-Oxygen Dynamics in the Tyrosinase Mechanism.
Fujieda N, Umakoshi K, Ochi Y, Nishikawa Y, Yanagisawa S, Kubo M, Kurisu G, Itoh S
Angew Chem Int Ed Engl 59 13385-13390 (2020)
PMID: 32356371

Function and Biology Details

Reaction catalysed: 
(1) L-tyrosine + O2 = L-dopaquinone + H2O.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tyrosinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 53.5 KDa
Source organism: Aspergillus oryzae
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1S9DK56 (Residues: 2-457; Coverage: 74%)
Gene name: OAory_01107480
Sequence domains: Common central domain of tyrosinase

Ligands and Environments

1 bound ligand:
Ligand NO3 1 x NO3
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P212121
Unit cell:
a: 54.277Å b: 104.747Å c: 154.321Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.161 0.219
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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