7BUY

The crystal structure of COVID-19 main protease in complex with carmofur

Summary for 7BUY

• Entry DOI: 10.2210/pdb7buy/pdb
• Descriptor: 3C-like proteinase, hexylcarbamic acid, DIMETHYL SULFOXIDE, ... (4 entities in total)
• Functional Keywords: covid-2019 virus, main protease, carmofur, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 1
• Total formula weight: 34361.41

Authors

Zhao, Y.,Zhang, B.,Jin, Z.,Liu, X.,Yang, H.,Rao, Z. (deposition date: 2020-04-08, release date: 2020-04-29, Last modification date: 2023-11-29)

Primary citation

Jin, Z.,Zhao, Y.,Sun, Y.,Zhang, B.,Wang, H.,Wu, Y.,Zhu, Y.,Zhu, C.,Hu, T.,Du, X.,Duan, Y.,Yu, J.,Yang, X.,Yang, X.,Yang, K.,Liu, X.,Guddat, L.W.,Xiao, G.,Zhang, L.,Yang, H.,Rao, Z.
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur.
Nat.Struct.Mol.Biol., 27:529-532, 2020

PubMed Abstract: The antineoplastic drug carmofur is shown to inhibit the SARS-CoV-2 main protease (M). Here, the X-ray crystal structure of M in complex with carmofur reveals that the carbonyl reactive group of carmofur is covalently bound to catalytic Cys145, whereas its fatty acid tail occupies the hydrophobic S2 subsite. Carmofur inhibits viral replication in cells (EC = 24.30 μM) and is a promising lead compound to develop new antiviral treatment for COVID-19.

PubMed: 32382072
DOI: 10.1038/s41594-020-0440-6

Experimental method

X-RAY DIFFRACTION (1.6 Å)