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Structure paper

TitleTwo adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure.
Journal, issue, pagesVirology, Vol. 388, Page 324-334, Year 2009
Publish dateNov 13, 2008 (structure data deposition date)
AuthorsHu, T. / Zhang, Y. / Li, L. / Wang, K. / Chen, S. / Chen, J. / Ding, J. / Jiang, H. / Shen, X.
External linksVirology / PubMed:19409595
MethodsX-ray diffraction
Resolution2.3 - 2.9 Å
Structure data

PDB-3f9e:
Crystal Structure of the S139A mutant of SARS-Coronovirus 3C-like Protease
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3f9f:
Crystal Structure of the F140A mutant of SARS-Coronovirus 3C-like Protease at pH 6.0
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3f9g:
Crystal Structure of the F140A mutant of SARS-Coronovirus 3C-like Protease at pH 6.5
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3f9h:
Crystal Structure of the F140A mutant of SARS-Coronovirus 3C-like Protease at pH 7.6
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • sars coronavirus
KeywordsHYDROLASE / protease / Cytoplasm / Membrane / Metal-binding / Ribosomal frameshifting / RNA-binding / Thiol protease / Transmembrane / Zinc / Zinc-finger

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