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. 2022 Mar 24;119(15):e2120913119. doi: 10.1073/pnas.2120913119

Fig. 2.

Fig. 2.

Two transient conformational of SARS-CoV-2 monomeric Mpro are captured by NB2B4 and NB1A2. (A) Crystal structure of SARS-CoV-2 monomeric Mpro in complex with NB2B4, with the monomeric Mpro colored in blue and NB2B4 colored in orange, respectively. SARS-CoV-2 monomeric Mpro presents an extended conformation. (B) Crystal structure of SARS-CoV-2 monomeric Mpro in complex with NB1A2, with the monomeric Mpro colored in cyan and NB1A2 colored in red, respectively. SARS-CoV-2 monomeric Mpro shows a compact conformation. (C) Superposition of the extended Mpro (blue) and active protomer of dimeric Mpro (magenta, PDB ID code 7LMC) based on the catalytic domain. (D) Superposition of the compact Mpro (cyan) and active protomer of dimeric Mpro (magenta, PDB ID code 7LMC). (E) The equilibrium among the extended monomers, the compact monomer, and the dimer of SARS-CoV-2 Mpro.