Fig. 4: Molecular docking studies with WT-CnTYR and the variant N201S.
WT-CnTYR and the variant N201S (homology modelled) with L-tyrosine 4, meta-L-tyrosine 9 and halogenated tyrosines 11 and 12 using AutoDock Vina35. a Docking of L-tyrosine 4 with the wild-type (WT) CnTYR and CnTYR-N201S: L-tyrosine 1 fits well into the active sites of WT-CnTYR and CnTYR-N201S. b Docking of meta-L-tyrosine 9 with the WT-CnTYR: 9 can fit into the active site of WT-CnTYR but not in a productive orientation. c Docking of 9 with CnTYR-N201S: 9 fits well into the active site of CnTYR-N201S. d Docking of 3-F-L-tyrosine 11 with WT-CnTYR and CnTYR-N201S: 11 fits well into the active site of both. e Docking of 3-Cl-L-tyrosine 12 with WT-CnTYR: 12 can fit into the active sites WT-CnTYR but not in a productive orientation. f Docking of 12 with CnTYR-N201S: 12 fits well into the active sites of CnTYR-N201S. The functional histamine residues in the tyrosinase active sites and substrates are shown in stick and ribbon forms. Enzyme residues are shown in tan. Compounds 4, 9, 11, and 12 are shown in grey, rose, blue, and light blue, respectively. The model of WT-CnTYR was generated by homology modelling (SWISS-MODEL)37 using the crystal structure of BmTYR (PDB code: 3NPY)36 as a template. CnTYR variants were generated and homology modelled by Chimera38,39,40.
