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. Author manuscript; available in PMC: 2024 Jul 14.

Published in final edited form as: ACS Infect Dis. 2023 Jun 30;9(7):1372–1386. doi: 10.1021/acsinfecdis.3c00125

Figure 6. — A) The fit of nirmatrelvir (left panel) and ensitrelvir (right panel) within the substrate envelope. The labeled M^pro positions are those that contain the 30 mutations with the highest DR scores. S1, G2, R4, N214, Q299 and C300 are located on monomer B (shown in darker gray) and are represented as cyan sticks. The S4-S3’ binding subsites are labeled in red. B) The number of nirmatrelvir and ensitrelvir resistance mutations at each position of M^pro. C) The number of nirmatrelvir and ensitrelvir resistance mutations at each position of M^pro are mapped to the M^pro-inhibitor structures. Inhibitors are shown in green.

Figure 6. — A) The fit of nirmatrelvir (left panel) and ensitrelvir (right panel) within the substrate envelope. The labeled M^pro positions are those that contain the 30 mutations with the highest DR scores. S1, G2, R4, N214, Q299 and C300 are located on monomer B (shown in darker gray) and are represented as cyan sticks. The S4-S3’ binding subsites are labeled in red. B) The number of nirmatrelvir and ensitrelvir resistance mutations at each position of M^pro. C) The number of nirmatrelvir and ensitrelvir resistance mutations at each position of M^pro are mapped to the M^pro-inhibitor structures. Inhibitors are shown in green.