1hqw
CRYSTAL STRUCTURE OF THE COMPLEX OF CONCANAVALIN A WITH A TRIPEPTIDE YPY
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OverviewOverview
The X-ray structure analysis of a cross-linked crystal of concanavalin A, soaked with the tripeptide molecule as the probe molecule showed electron, density corresponding to full occupation in the binding pocket. The site, lies on the surface of concanavalin A and is surrounded by three, symmetry-related molecules. The crystal structure of the tripeptide, complex was refined at 2.4-A resolution to an R-factor of 17.5%, (Rfree, factor of 23.7%), with an RMS deviation in bond distances of 0.01 A. The, model includes all 237 residue of concanavalin A, 1 manganese ion, 1, calcium ion, 161 water molecules, 1 glutaraldehyde molecule, and 1, tripeptide molecule. This X-ray structure analysis also provides an, approach to mapping the binding surface of crystalline protein with a, probe molecule that is dissolved in a mixture of organic solvent with, water or in neat organic solvent but is hardly dissolved in aqueous, solution.
About this StructureAbout this Structure
1HQW is a Single protein structure of sequence from Canavalia ensiformis with MN, CA and PTD as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the complex of concanavalin A and tripeptide., Zhang Z, Qian M, Huang Q, Jia Y, Tang Y, Wang K, Cui D, Li M, J Protein Chem. 2001 Jan;20(1):59-65. PMID:11330349
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