Structure of PEDV main protease bound to potent broad-spectrum non-covalent inhibitor X77

2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.

Center for Structural Genomics of Infectious Diseases (CSGID)

DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID; METHANEDICARBOXYLIC ACID

A taxonomically-driven approach to development of potent, broad-spectrum inhibitors of coronavirus main protease including SARS-CoV-2 (COVID-19)

AGLRKMAQPSGVVEKCIVRVCYGNMALNGLWLGDTVICPRHVIASSTTSTIDYDYALSVLRLHNFSISSGNVFLGVVGVT
MRGALLQIKVNQNNVHTPKYTYRTVRPGESFNILACYDGSAAGVYGVNMRSNYTIRGSFINGACGSPGYNINNGTVEFCY
LHQLELGSGCHVGSDLDGVMYGGYEDQPTLQVEGASSLFTENVLAFLYAALINGSTWWLSSSRIAVDRFNEWAVHNGMTT
VVNTDCFSILAAKTGVDVQRLLASIQSLHKNFGGKQILGYTSLTDEFTTGEVIRQMYGVNLQ

PEDV-3CLpro:77 inhibitor complex was co-crystallized by setting up 2 uL drops that were composed of 1 uL of purified PEDV-3CLpro (2.4 mg/mL) that had been incubated for three hours with a 3 molar excess of compound 77, and 1 uL of reservoir solution: 0.20 M malonic acid (MIB) pH 4.0 and 25% PEG-3350

Center for Structural Genomics of Infectious Diseases
NIAID, National Institute of Allergy and Infectious Diseases

National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)

SARS main protease bound to inhibitor X77

COVID-19 main protease bound to inhibitor X77

PEDV 3CLpro aka main protease runs as a dimer on a SEC column

COVID-19, porcine epidemic diarrhea virus, PEDV, main protease, 3C-like protease, 3CL protease, 3Clpro, Mpro, broad-spectrum, inhibitor, proteinase, non-covalent, reversible, Structural Genomics, Center for Structural Genomics of Infectious Diseases, CSGID, ANTIVIRAL PROTEIN, VIRAL PROTEIN, VIRAL PROTEIN-INHIBITOR complex