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Reassembled Neuraminidase Type N9

From Avian Influenza Virus (n1_7NN9.pdb)

(Display produced using JSmol and HTML5. If you don't see a structure try a different browser.)

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View chain A down the beta-sheet barrel (aka Propeller Axis). The catalytically important phenolic oxygen of Tyr406 shown in red.
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As with other enzymes, the catalytic site is enclosed and physically constrained. This enzyme acts on the terminal residue of an oligosaccharide and therefore must provide a passageway through which the oligosaccharide can extend from the outside to the active site. The passageway is most likely at each point of meeting of 3 subunits. Constraint is produced by the focussed compressive stress of four barrels. The orientation of the barrels deviates from a regular tetrahedron to provide the optimum spatial distribution of stress for catalysis at the active site.

For further information about this protein, see posts of 15 April 2015 and 14 April 2007 on nativeproteins.blogspot.com

Or contact the author, Dr Don Vanselow at dvanselow@hotmail.com

Further details of JSmol available here