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-Structure paper
Title | Influenza neuraminidase operates via a nucleophilic mechanism and can be targeted by covalent inhibitors |
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Journal, issue, pages | Nat Commun, Vol. 4, Page 1491-1491, Year 2013 |
Publish date | Sep 18, 2012 (structure data deposition date) |
Authors | Vavricka, C.J. / Liu, Y. / Kiyota, H. / Sriwilaijaroen, N. / Qi, J. / Tanaka, K. / Wu, Y. / Li, Q. / Li, Y. / Yan, J. ...Vavricka, C.J. / Liu, Y. / Kiyota, H. / Sriwilaijaroen, N. / Qi, J. / Tanaka, K. / Wu, Y. / Li, Q. / Li, Y. / Yan, J. / Suzuki, Y. / Gao, G.F. |
External links | Nat Commun / PubMed:23422659 |
Methods | X-ray diffraction |
Resolution | 1.5 - 1.803 Å |
Structure data | PDB-4h52: PDB-4h53: |
Chemicals | ChemComp-CA: ChemComp-FSI: ChemComp-HOH: ChemComp-NAG: ChemComp-SLB: ChemComp-GOL: |
Source |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / NEURAMINIDASE / INFLUENZA SURFACE GLYCOPROTEIN / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex / INFLUENZA VIRUS SURFACE |