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5L15

The crystal structure of neuraminidase in complex with oseltamivir from A/Shanghai/2/2013 (H7N9) influenza virus

Summary for 5L15
Entry DOI10.2210/pdb5l15/pdb
Related5L14 5L17 5L18
DescriptorNeuraminidase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordsneuraminidase, h7n9, hydrolase
Biological sourceInfluenza A virus
Cellular locationHost apical cell membrane ; Single-pass type II membrane protein : R4NFR6
Total number of polymer chains1
Total formula weight46360.18
Authors
Yang, H.,Stevens, J. (deposition date: 2016-07-28, release date: 2017-08-09, Last modification date: 2024-11-06)
Primary citationGubareva, L.V.,Sleeman, K.,Guo, Z.,Yang, H.,Hodges, E.,Davis, C.T.,Baranovich, T.,Stevens, J.
Drug Susceptibility Evaluation of an Influenza A(H7N9) Virus by Analyzing Recombinant Neuraminidase Proteins.
J. Infect. Dis., 216:S566-S574, 2017
Cited by
PubMed Abstract: Neuraminidase (NA) inhibitors are the recommended antiviral medications for influenza treatment. However, their therapeutic efficacy can be compromised by NA changes that emerge naturally and/or following antiviral treatment. Knowledge of which molecular changes confer drug resistance of influenza A(H7N9) viruses (group 2NA) remains sparse.
PubMed: 28934455
DOI: 10.1093/infdis/jiw625
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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