Literature summary for 3.2.1.18 extracted from

Malaisree, M.; Rungrotmongkol, T.; Decha, P.; Intharathep, P.; Aruksakunwong, O.; Hannongbua, S.
Understanding of known drug-target interactions in the catalytic pocket of neuraminidase subtype N1 (2008), Proteins, 71, 1908-1918.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulation study of inhibitors oseltamivir, zanamivir and peramivir embedded in the catalytic site. In comparison with oseltamivir and zanamivir, peramivir shows strong direct ligand-enzyme hydrogen bonding, less space available in the N1 pocket, and it interacts tightly, via its OH group, with the D51 residue located in the 150-loop region	unidentified influenza virus

Inhibitors

Inhibitors	Comment	Organism	Structure
oseltamivir	molecular dynamics simulation study. In comparison with oseltamivir and zanamivir, peramivir shows strong direct ligand-enzyme hydrogen bonding, less space available in the N1 pocket, and it interacts tightly, via its OH group, with the D51 residue located in the 150-loop region	unidentified influenza virus
peramivir	molecular dynamics simulation study	unidentified influenza virus
zanamivir	molecular dynamics simulation study	unidentified influenza virus

Organism

Organism	UniProt	Comment	Textmining
unidentified influenza virus	-	H5N1 avian influenza virus	-

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Release 2023.1 (January 2023)