7BRO
Crystal structure of the 2019-nCoV main protease
Summary for 7BRO
| Entry DOI | 10.2210/pdb7bro/pdb |
| Descriptor | 3C-like proteinase (2 entities in total) |
| Functional Keywords | 2019-ncov main protease, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 1 |
| Total formula weight | 33882.60 |
| Authors | Fu, L.F. (deposition date: 2020-03-29, release date: 2020-05-13, Last modification date: 2023-11-29) |
| Primary citation | Fu, L.,Ye, F.,Feng, Y.,Yu, F.,Wang, Q.,Wu, Y.,Zhao, C.,Sun, H.,Huang, B.,Niu, P.,Song, H.,Shi, Y.,Li, X.,Tan, W.,Qi, J.,Gao, G.F. Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease. Nat Commun, 11:4417-4417, 2020 Cited by PubMed Abstract: COVID-19 was declared a pandemic on March 11 by WHO, due to its great threat to global public health. The coronavirus main protease (M, also called 3CLpro) is essential for processing and maturation of the viral polyprotein, therefore recognized as an attractive drug target. Here we show that a clinically approved anti-HCV drug, Boceprevir, and a pre-clinical inhibitor against feline infectious peritonitis (corona) virus (FIPV), GC376, both efficaciously inhibit SARS-CoV-2 in Vero cells by targeting M. Moreover, combined application of GC376 with Remdesivir, a nucleotide analogue that inhibits viral RNA dependent RNA polymerase (RdRp), results in sterilizing additive effect. Further structural analysis reveals binding of both inhibitors to the catalytically active side of SARS-CoV-2 protease M as main mechanism of inhibition. Our findings may provide critical information for the optimization and design of more potent inhibitors against the emerging SARS-CoV-2 virus. PubMed: 32887884DOI: 10.1038/s41467-020-18233-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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