1con
|
THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION
OverviewOverview
The three-dimensional structure of cadmium-substituted concanavalin A has, been refined using X-PLOR. The R factor on all data between 8 and 2 A is, 17.1%. The protein crystallizes in space group I222 with cell dimensions a, = 88.7, b = 86.5 and c = 62.5 A and has one protein subunit per asymmetric, unit. The final structure contains 237 amino acids, two Cd ions, one Ca, ion and 144 water molecules. One Cd ion occupies the transition-metal, binding site and the second occupies an additional site, the coordinates, of which were first reported by Weinzierl & Kalb [FEBS Lett. (1971), 18, 268-270]. The additional Cd ion is bound with distorted octahedral, symmetry and bridges the cleft between the two monomers which form the, conventional dimer of concanavalin A. This study provides a detailed, analysis of the refined structure of saccharide-free concanavalin A and is, the basis for comparison with saccharide complexes reported elsewhere.
About this StructureAbout this Structure
1CON is a Single protein structure of sequence from Canavalia ensiformis with CD and CA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Refined structure of cadmium-substituted concanavalin A at 2.0 A resolution., Naismith JH, Habash J, Harrop S, Helliwell JR, Hunter WN, Wan TC, Weisgerber S, Kalb AJ, Yariv J, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):561-71. PMID:15299493
Page seeded by OCA on Tue Nov 20 12:37:48 2007