1HQW

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

1HQW の概要

• エントリーDOI: 10.2210/pdb1hqw/pdb
• 分子名称: CONCANAVALIN A, YPY, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: beta sheets, lectin binding
• 由来する生物種: Canavalia ensiformis (jack bean); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26258.99

構造登録者

Zhang, Z.,Qian, M.,Huang, Q.,Jia, Y.,Tang, Y.,Wang, K.,Cui, D.,Li, M. (登録日: 2000-12-20, 公開日: 2003-10-07, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)