Fig. 9: Structural basis for the Mpro inhibition.
From: Identification of SARS-CoV-2 inhibitors targeting Mpro and PLpro using in-cell-protease assay
a Crystal structure of the Mpro and MG-101 complex. Mpro dimer is depicted as a cartoon model with a transparent surface and each protomer is colored green and pink. MG-101 is shown as CPK representation. b Electron density map (2Fo–Fc, blue mesh) of MG-101 bound at the active site of Mpro. The inhibitor and Mpro are depicted as ball-and-stick and wire models, respectively. A thiohemiacetal covalent between the inhibitor and C145 residue of Mpro is indicated by a red arrow. c Interactions between the inhibitor and active site of Mpro. The binding of MG-101 is stabilized by H-bonds (black dot lines) with Gly143, Cys145, His164, and Glu166. d Comparison of the binding of MG-101 (orange) and GC373 (cyan) at the active site of Mpro. S1–S3 subsites of Mpro and P1–P3 of inhibitors are indicated.
