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TitleSevere acute respiratory syndrome coronavirus nsp9 dimerization is essential for efficient viral growth
Journal, issue, pagesJ. Virol., Vol. 83, Page 3007-3018, Year 2009
Publish dateSep 4, 2008 (structure data deposition date)
AuthorsMiknis, Z.J. / Donaldson, E.F. / Umland, T.C. / Rimmer, R.A. / Baric, R.S. / Schultz, L.W.
External linksJ. Virol. / PubMed:19153232
MethodsX-ray diffraction
Resolution2.6 Å
Structure data

PDB-3ee7:
Crystal Structure of SARS-CoV nsp9 G104E
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • sars coronavirus
KeywordsVIRAL PROTEIN / GXXXG / DIMERIZATION / SARS-COV / HELIX-HELIX / Hydrolase / Membrane / Metal-binding / Protease / RNA-binding / Thiol protease / Transmembrane / Zinc-finger

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