On https://www.uniprot.org/uniprot/P07524, tyrosinase is shown as a monophenol monooxygenase. However, the UniProt database only shows a metal (copper) binding site, when there is presumed to be an actual active site that performs the reactions, other than the metal binding site. Are there any clues to find the actual reaction active site for a monooxygenase? Please include the sources, if there are.
Tyrosinase uses two copper ions as cofactors. The copper binding site is the enzyme active site.
The active site of the crystal structure of tyrosinase from Streptomyces sp. (PDB code: 3AWT) is shown below. Note the two copper ions (coordinated by active site histidine amino acid residues) and an oxygen atom (of a water molecule) bound to the copper ions:
The Cu(II)-soaked crystal structure of tyrosinase ... possesses two copper ions at its catalytic center.