5WKK
1.55 A resolution structure of MERS 3CL protease in complex with inhibitor GC813
Summary for 5WKK
| Entry DOI | 10.2210/pdb5wkk/pdb |
| Descriptor | Orf1a protein, TETRAETHYLENE GLYCOL, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | protease, protease inhhibitors, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Middle East respiratory syndrome-related coronavirus |
| Total number of polymer chains | 1 |
| Total formula weight | 35600.82 |
| Authors | Lovell, S.,Battaile, K.P.,Mehzabeen, N.,Kankanamalage, A.C.G.,Kim, Y.,Rathnayake, A.D.,Chang, K.O.,Groutas, W.C. (deposition date: 2017-07-25, release date: 2018-04-04, Last modification date: 2024-10-30) |
| Primary citation | Galasiti Kankanamalage, A.C.,Kim, Y.,Damalanka, V.C.,Rathnayake, A.D.,Fehr, A.R.,Mehzabeen, N.,Battaile, K.P.,Lovell, S.,Lushington, G.H.,Perlman, S.,Chang, K.O.,Groutas, W.C. Structure-guided design of potent and permeable inhibitors of MERS coronavirus 3CL protease that utilize a piperidine moiety as a novel design element. Eur J Med Chem, 150:334-346, 2018 Cited by PubMed Abstract: There are currently no approved vaccines or small molecule therapeutics available for the prophylaxis or treatment of Middle East Respiratory Syndrome coronavirus (MERS-CoV) infections. MERS-CoV 3CL protease is essential for viral replication; consequently, it is an attractive target that provides a potentially effective means of developing small molecule therapeutics for combatting MERS-CoV. We describe herein the structure-guided design and evaluation of a novel class of inhibitors of MERS-CoV 3CL protease that embody a piperidine moiety as a design element that is well-suited to exploiting favorable subsite binding interactions to attain optimal pharmacological activity and PK properties. The mechanism of action of the compounds and the structural determinants associated with binding were illuminated using X-ray crystallography. PubMed: 29544147DOI: 10.1016/j.ejmech.2018.03.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
Download full validation report
