9PJG
SARS-CoV2 Mpro bound to compound 1
Summary for 9PJG
| Entry DOI | 10.2210/pdb9pjg/pdb |
| Descriptor | 3C-like proteinase nsp5, (P6S)L(ELL) peptide (3 entities in total) |
| Functional Keywords | coronavirus, protease, inhibitor, 3clpro, sars-cov2, viral protein, viral protein-inhibitor complex, viral protein/inhibitor |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 4 |
| Total formula weight | 68458.04 |
| Authors | Campbell, A.C.,Opel-Reading, H.K.,Krause, K.L. (deposition date: 2025-07-14, release date: 2025-12-31) |
| Primary citation | Brimble, M.A.,Stubbing, L.A.,Hermant, Y.O.,Yang, S.H.,Hubert, J.G.,Pearl, E.S.,McSweeney, A.M.,Young, V.L.,Campbell, A.C.,Opel-Reading, H.K.,McKenzie-Goldsmith, G.M.,Putha, L.,Mortuza, R.,Wang, H.,Hurst, B.L.,Julander, J.,Harris, L.D.,Krause, K.L.,Ward, V.K. Broad-Spectrum Peptidomimetic Inhibitors of Norovirus and Coronavirus 3C-like Proteases. Acs Infect Dis., 2025 Cited by PubMed Abstract: The cysteine 3C-like proteases (3CL) of caliciviruses, coronaviruses, and picornaviruses are essential for viral replication. In this study, we report the development of potent broad-spectrum peptidomimetic antiviral agents that target the 3CL of caliciviruses (NS6), coronaviruses (M), and a picornavirus (3C). Based upon previously reported inhibitors, a small library of compounds was designed, synthesized and tested to identify a core structure, which was then derivatized with a focus upon P3 and P4 positions to afford new inhibitors with improved potency against the respective viral enzymes and enhanced binding as determined by X-ray crystallography. These compounds were tested against a range of viruses in culture, revealing minimal toxicity while exhibiting broad-spectrum potent nanomolar activities against noroviruses and several coronavirus species, including alpha and omicron variants of SARS-CoV-2 and Middle East Respiratory Syndrome virus (MERS). PubMed: 41412823DOI: 10.1021/acsinfecdis.5c00680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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