Structural highlights
Function
CONA_CANEN D-mannose specific lectin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The correct positions of the deuterium (D) atoms of many of the bound waters in the protein concanavalin A are revealed by neutron Laue diffraction. The approach includes cases where these water D atoms show enough mobility to render them invisible even to ultra-high resolution synchrotron-radiation X-ray crystallography. The positions of the bound water H atoms calculated on the basis of chemical and energetic considerations are often incorrect. The D-atom positions for the water molecules in the Mn-, Ca- and sugar-binding sites of concanavalin A are described in detail.
Direct determination of the positions of the deuterium atoms of the bound water in -concanavalin A by neutron Laue crystallography.,Habash J, Raftery J, Nuttall R, Price HJ, Wilkinson C, Kalb AJ, Helliwell JR Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):541-50. PMID:10771422[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Habash J, Raftery J, Nuttall R, Price HJ, Wilkinson C, Kalb AJ, Helliwell JR. Direct determination of the positions of the deuterium atoms of the bound water in -concanavalin A by neutron Laue crystallography. Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):541-50. PMID:10771422
