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TitleStructures of two coronavirus main proteases: implications for substrate binding and antiviral drug design.
Journal, issue, pagesJ. Virol., Vol. 82, Page 2515-2527, Year 2008
Publish dateJun 4, 2007 (structure data deposition date)
AuthorsXue, X. / Yu, H. / Yang, H. / Xue, F. / Wu, Z. / Shen, W. / Li, J. / Zhou, Z. / Ding, Y. / Zhao, Q. ...Xue, X. / Yu, H. / Yang, H. / Xue, F. / Wu, Z. / Shen, W. / Li, J. / Zhou, Z. / Ding, Y. / Zhao, Q. / Zhang, X.C. / Liao, M. / Bartlam, M. / Rao, Z.
External linksJ. Virol. / PubMed:18094151
MethodsX-ray diffraction
Resolution2 - 2.5 Å
Structure data

PDB-2q6d:
Crystal structure of infectious bronchitis virus (IBV) main protease
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-2q6f:
Crystal structure of infectious bronchitis virus (IBV) main protease in complex with a Michael acceptor inhibitor N3
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2q6g:
Crystal structure of SARS-CoV main protease H41A mutant in complex with an N-terminal substrate
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • infectious bronchitis virus
  • synthetic construct (others)
  • sars coronavirus
KeywordsHYDROLASE / coronavirus; IBV; main protease; 3C-Like proteinase / coronavirus; IBV; main protease; 3C-Like proteinase; Michael acceptor inhibitor / coronavirus; SARS-CoV; main protease; 3C-Like proteinase;substrate

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