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1nn2, resolution 2.20Å ()
Ligands: , , , ,
Non-Standard Residues:
Activity: Exo-alpha-sialidase, with EC number
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Publication Abstract from PubMed

An atomic model of the tetrameric surface glycoprotein neuraminidase of influenza virus A/Tokyo/3/67 has been built and refined based on X-ray diffraction data at 2.2 A resolution. The crystallographic residual is 0.21 for data between 6 and 2.2 A resolution and the r.m.s. deviations from ideal geometry are 0.02 A for bond lengths and 3.9 degrees for bond angles. The model includes amino acid residues 83 to 469, four oligosaccharide structures N-linked at asparagine residues 86, 146, 200 and 234, a single putative Ca2+ ion site, and 85 water molecules. One of the oligosaccharides participates in a novel crystal contact. The folding pattern is a beta-sheet propeller as described earlier and details of the intramolecular interactions between the six beta-sheets are presented. Strain-invariant residues are clustered around the propeller axis on the upper surface of the molecule where they line the wall of a cavity into which sialic has been observed to bind. Strain-variable residues implicated in binding to antibodies surround this site.

Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution., Varghese JN, Colman PM, J Mol Biol. 1991 Sep 20;221(2):473-86. PMID:1920428

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1nn2 is a 1 chain structure with sequence from Viruses. The May 2009 RCSB PDB Molecule of the Month feature on Influenza Neuraminidase by David Goodsell is 10.2210/rcsb_pdb/mom_2009_5. Full crystallographic information is available from OCA.

See Also


  • Varghese JN, Colman PM. Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. J Mol Biol. 1991 Sep 20;221(2):473-86. PMID:1920428

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