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TitleLigand-induced Dimerization of Middle East Respiratory Syndrome (MERS) Coronavirus nsp5 Protease (3CLpro): IMPLICATIONS FOR nsp5 REGULATION AND THE DEVELOPMENT OF ANTIVIRALS.
Journal, issue, pagesJ. Biol. Chem., Vol. 290, Page 19403-19422, Year 2015
Publish dateNov 10, 2014 (structure data deposition date)
AuthorsTomar, S. / Johnston, M.L. / St John, S.E. / Osswald, H.L. / Nyalapatla, P.R. / Paul, L.N. / Ghosh, A.K. / Denison, M.R. / Mesecar, A.D.
External linksJ. Biol. Chem. / PubMed:26055715
MethodsX-ray diffraction
Resolution1.62 - 2.1 Å
Structure data

PDB-4rsp:
X-ray structure of MERS-CoV nsp5 protease bound with a designed inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

PDB-4ylu:
X-ray structure of MERS-CoV nsp5 protease bound with a non-covalent inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-R30:
N-{4-[(1H-benzotriazol-1-ylacetyl)(thiophen-3-ylmethyl)amino]phenyl}propanamide

ChemComp-ACT:
ACETATE ION

Source
  • middle east respiratory syndrome coronavirus
KeywordsHydrolase/hydrolase Inhibitor / protease / Hydrolase-hydrolase Inhibitor complex

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