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. 2021 Jan 20;12:488. doi: 10.1038/s41467-020-20718-8

Fig. 2. Structural and mechanistic analysis of SARS-CoV-2 PLproC111S in complex with GRL0617, and in comparison with SARS-CoV and MERS PLpro.

Fig. 2

a Surface and cartoon structures of SARS-CoV-2 PLpro in complex with GRL0617 (orange sticks) showing the N-terminal UBL domain (magenta) and C-terminal USP domain (marine). b The binding pocket of GRL0617 in PLpro. The PLpro residues involved in GRL0617 binding are shown as marine sticks. The 2Fo-Fc omit map (contour level = 1.6 σ, shown as purple mesh). c Schematic diagram of SARS-CoV-2 PLproC111S/GRL0617 interactions shown in (b). d Comparison of GRL0617-bound (marine) PLproC111S and unbound (cyan) PLproC111S (PDB ID: 6WRH [10.2210/pdb6wrh/pdb]) structures. Y268 and Q269 on the BL2 loop shifted toward GRL0617 upon binding. GRL0617 shown as orange sticks; the catalytic triad residues (S111 in place of C111, H272, and D286) are shown in yellow; Y268 and Q269 are shown in marine in bound state, and in cyan in unbound state. e Comparisons of the binding sites of SARS-CoV PLpro/GRL0617 (slate sticks, PDB ID: 3E9S [10.2210/pdb3e9s/pdb])26, SARS-CoV-2 PLproC111S/GRL0617 (marine sticks), and MERS-CoV PLpro (deep teal sticks, PDB ID: 4RNA [10.2210/pdb4rna/pdb])37.