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Structure paper

TitleInvestigation of flexibility of neuraminidase 150-loop using tamiflu derivatives in influenza A viruses H1N1 and H5N1.
Journal, issue, pagesBioorg. Med. Chem., Vol. 27, Page 2935-2947, Year 2019
Publish dateSep 19, 2018 (structure data deposition date)
AuthorsZima, V. / Albinana, C.B. / Rojikova, K. / Pokorna, J. / Pachl, P. / Rezacova, P. / Hudlicky, J. / Navratil, V. / Majer, P. / Konvalinka, J. ...Zima, V. / Albinana, C.B. / Rojikova, K. / Pokorna, J. / Pachl, P. / Rezacova, P. / Hudlicky, J. / Navratil, V. / Majer, P. / Konvalinka, J. / Kozisek, M. / Machara, A.
External linksBioorg. Med. Chem. / PubMed:31128993
MethodsX-ray diffraction
Resolution1.88 Å
Structure data

PDB-6hp0:
Complex of Neuraminidase from H1N1 Influenza Virus in Complex with Oseltamivir Triazol Derivative
Method: X-RAY DIFFRACTION / Resolution: 1.88 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-GJT:
(3~{R},4~{R},5~{S})-4-acetamido-5-[4-(hydroxymethyl)-1,2,3-triazol-1-yl]-3-pentan-3-yloxy-cyclohexene-1-carboxylic acid

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

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-HOH:
WATER

Source
  • influenza a virus (a/texas/17/2009(h1n1))
KeywordsVIRAL PROTEIN / neuraminidase / influenza / complex / inhibitor

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