Fig. 3: Mpro L50F single mutant crystal structure with unique substrate binding mode.
From: Distal protein-protein interactions contribute to nirmatrelvir resistance
a L50F single mutant dimer of a dimer (yellow/wheat, blue/light blue), showing P1–P6 (light blue) of the C-terminus bound in the chain B (wheat) active site. The zoomed-in view shows the interactions of the enzyme F50 with the substrate hydrophobic pocket. A view of the chain A interactions can be found in Supplementary Fig. 4. Mutation is noted in red text. b Binding of P1–P6 in the L50F chain B active site. The substrate protomer is shown in light blue, and the enzyme protomer is shown in wheat. The mutation is noted in red text. c Comparison of the binding modes of P1–P6 in the L50F single mutant (light blue/wheat) vs. the L50F/E166A/L167F triple mutant (magenta/green). Mutations are noted in red text.
