1CON

THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION

Summary for 1CON

• Entry DOI: 10.2210/pdb1con/pdb
• Descriptor: CONCANAVALIN A, CADMIUM ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: lectin(agglutinin)
• Biological source: Canavalia ensiformis (jack bean)
• Total number of polymer chains: 1
• Total formula weight: 25887.28

Authors

Naismith, J.H.,Habash, J.,Harrop, S.J.,Helliwell, J.R.,Hunter, W.N.,Kalb(Gilboa), A.J.,Yariv, J.,Wan, T.C.M.,Weisgerber, S. (deposition date: 1993-03-16, release date: 1994-01-31, Last modification date: 2024-02-07)

Primary citation

Naismith, J.H.,Habash, J.,Harrop, S.,Helliwell, J.R.,Hunter, W.N.,Wan, T.C.,Weisgerber, S.,Kalb, A.J.,Yariv, J.
Refined structure of cadmium-substituted concanavalin A at 2.0 A resolution.
Acta Crystallogr.,Sect.D, 49:561-571, 1993

PubMed Abstract: 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.

PubMed: 15299493
DOI: 10.1107/S0907444993006390

Experimental method

X-RAY DIFFRACTION (2 Å)