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3NSS

The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active sites

Summary for 3NSS
Entry DOI10.2210/pdb3nss/pdb
Related3BEQ
DescriptorNeuraminidase, alpha-D-mannopyranose-(1-3)-alpha-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 Keywords6-bladed beta-propeller, hydrolase, calcium binding, glycosylation
Biological sourceInfluenza A virus
Cellular locationVirion membrane: C3W5S3
Total number of polymer chains2
Total formula weight87304.13
Authors
Li, Q.,Qi, J.X.,Zhang, W.,Vavricka, C.J.,Shi, Y.,Gao, G.F. (deposition date: 2010-07-02, release date: 2010-09-22, Last modification date: 2024-10-30)
Primary citationLi, Q.,Qi, J.X.,Zhang, W.,Vavricka, C.J.,Shi, Y.,Wei, J.H.,Feng, E.G.,Shen, J.S.,Chen, J.L.,Liu, D.,He, J.H.,Yan, J.H.,Liu, H.,Jiang, H.L.,Teng, M.K.,Li, X.B.,Gao, G.F.
The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site
Nat.Struct.Mol.Biol., 17:1266-1268, 2010
Cited by
PubMed Abstract: Influenza A virus neuraminidase can be classified into groups 1 and 2 on the basis of its primary structure. The main structural feature of group 1 neuraminidase is an extra cavity in the active site, the 150-cavity. Here we present the crystal structure of neuraminidase from the 2009 pandemic H1N1 influenza strain. In contrast to other characterized N1 neuraminidases, which are all members of group 1, 2009 H1N1 neuraminidase does not have a 150-cavity.
PubMed: 20852645
DOI: 10.1038/nsmb.1909
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.902 Å)
Structure validation

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