5C3N

Crystal structure of MERS coronavirus main protease in spacegroup C2221

Summary for 5C3N

Entry DOI	10.2210/pdb5c3n/pdb
Descriptor	ORF1a protein (1 entity in total)
Functional Keywords	mers coronavirus, main protease, 3cl protease, hydrolase
Biological source	Middle East respiratory syndrome coronavirus
Total number of polymer chains	2
Total formula weight	66708.34
Authors	Chou, C.Y.,Cheng, S.C. (deposition date: 2015-06-17, release date: 2015-12-30, Last modification date: 2023-11-08)
Primary citation	Ho, B.L.,Cheng, S.C.,Shi, L.,Wang, T.Y.,Ho, K.I.,Chou, C.Y. Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease. Plos One, 10:e0144865-e0144865, 2015 Cited by PubMed Abstract: A highly pathogenic human coronavirus (CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), has emerged in Jeddah and other places in Saudi Arabia, and has quickly spread to European and Asian countries since September 2012. Up to the 1st October 2015 it has infected at least 1593 people with a global fatality rate of about 35%. Studies to understand the virus are necessary and urgent. In the present study, MERS-CoV main protease (Mpro) is expressed; the dimerization of the protein and its relationship to catalysis are investigated. PubMed: 26658006 DOI: 10.1371/journal.pone.0144865 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3 Å)

Structure validation