Skip to main content
. 2024 Jan 17;19(2):563–574. doi: 10.1021/acschembio.3c00720

Figure 5.

Figure 5

CSP plots of Z604 (purple), 30b (light blue), 30c (red), 31c (green), 32a (orange), and 35b (pink) (a). The light-pink shade shows the active site amino acids with the indication of the subpockets (exemplary amino acids for S1’: T24, T25, T26, L27, S1: F140, L141, N142, G143, S144, C145, H163, H164, S2: C44, T45, S46, E47, M49, S3: L167, P168, G170, T190, Q192). Exemplary CSPs of V42 and G174 in the absence (black) and presence of ligands are shown in (b). See also Figures S9–S10 for the reference compounds. Modeling of each ligand within the active site pocket of Mpro ((c) left column: noncovalent; right column: covalent binding). Amino acids N142 and Q189 are removed for visibility of the active site pockets (see Figure S11 for the same structures with all amino acids). The cocrystal structure of Mpro with two 35b binding sites (PDB: 8PH4) shown as a dimer with indication of first (black rectangle) and second binding sites (red). A section of the active site is shown in the same position as in (c) and when tilted to show all moieties within the pocket (d). Overlay of all modeled ligands with the indication of subpockets (e). KD determination derived from combined CSPs for the first (left) and second binding sites of 35b (right) (f).