Fig. 3

a Difference in the molecular surface near Y220 position in p53^WT and p53^Y220C mutant. a Size of cavity in p53^WT. b Mutation from Tyr to Cys at 220th position rearranges the conformation of surrounding residues, especially located in the loop region. Widening of the loop near 220th position and removal of the Tyr side chain creates a larger cavity in p53^Y220C protein. c Superimposition of the two molecular surfaces reveals the stringency of the p53^WT (green color) as compared to the p53^Y220C (red color). b Water network near 220th residue in p53^WT and p53^Y220C protein. a Tyr 220 stabilizes the residues of surrounding loops with the help of water molecules. b Cys 220 stabilizes the cavity by solvating it with water molecules. Binding of the withanolides with p53^WT near Tyr 220. Wi-A c and Wi-N d were found to interact with the surface residues near Tyr 220 as no deep cavity was present in p53^WT