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Structure paper

TitleInfluenza neuraminidase operates via a nucleophilic mechanism and can be targeted by covalent inhibitors
Journal, issue, pagesNat Commun, Vol. 4, Page 1491-1491, Year 2013
Publish dateSep 18, 2012 (structure data deposition date)
AuthorsVavricka, 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 linksNat Commun / PubMed:23422659
MethodsX-ray diffraction
Resolution1.5 - 1.803 Å
Structure data

PDB-4h52:
Wild-type influenza N2 neuraminidase covalent complex with 3-fluoro-Neu5Ac
Method: X-RAY DIFFRACTION / Resolution: 1.803 Å

PDB-4h53:
Influenza N2-Tyr406Asp neuraminidase in complex with beta-Neu5Ac
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-FSI:
5-acetamido-3,5-dideoxy-3-fluoro-D-erythro-alpha-L-manno-non-2-ulopyranosonic acid

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-SLB:
N-acetyl-beta-neuraminic acid

ChemComp-GOL:
GLYCEROL

Source
  • influenza a virus
KeywordsHYDROLASE/HYDROLASE INHIBITOR / NEURAMINIDASE / INFLUENZA SURFACE GLYCOPROTEIN / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex / INFLUENZA VIRUS SURFACE

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