1HQW

CRYSTAL STRUCTURE OF THE COMPLEX OF CONCANAVALIN A WITH A TRIPEPTIDE YPY

Summary for 1HQW

• Entry DOI: 10.2210/pdb1hqw/pdb
• Descriptor: CONCANAVALIN A, YPY, MANGANESE (II) ION, ... (6 entities in total)
• Functional Keywords: beta sheets, lectin binding
• Biological source: Canavalia ensiformis (jack bean); More
• Total number of polymer chains: 2
• Total formula weight: 26258.99

Authors

Zhang, Z.,Qian, M.,Huang, Q.,Jia, Y.,Tang, Y.,Wang, K.,Cui, D.,Li, M. (deposition date: 2000-12-20, release date: 2003-10-07, Last modification date: 2024-03-13)

Primary citation

Zhang, Z.,Qian, M.,Huang, Q.,Jia, Y.,Tang, Y.,Wang, K.,Cui, D.,Li, M.
Crystal structure of the complex of concanavalin A and tripeptide
J.PROTEIN CHEM., 20:59-65, 2001

PubMed Abstract: 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.

PubMed: 11330349
DOI: 10.1023/A:1011053330536

Experimental method

X-RAY DIFFRACTION (2.4 Å)