The structure of the saccharide-binding site of concanavalin A.

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Abstract
A complex of concanavalin A with methyl alpha‐D‐mannopyranoside has been crystallized in space group P212121 with a = 123.9 A, b = 129.1 A and c = 67.5 A. X‐ray diffraction intensities to 2.9 A resolution have been collected on a Xentronics/Nicolet area detector. The structure has been solved by molecular replacement where the starting model was based on refined coordinates of an I222 crystal of saccharide‐free concanavalin A. The structure of the saccharide complex was refined by restrained least‐squares methods to an R‐factor value of 0.19. In this crystal form, the asymmetric unit contains four protein subunits, to each of which a molecule of mannoside is bound in a shallow crevice near the surface of the protein. The methyl alpha‐D‐mannopyranoside molecule is bound in the C1 chair conformation 8.7 A from the calcium‐binding site and 12.8 A from the transition metal‐binding site. A network of seven hydrogen bonds connects oxygen atoms O‐3, O‐4, O‐5 and O‐6 of the mannoside to residues Asn14, Leu99, Tyr100, Asp208 and Arg228. O‐2 and O‐1 of the mannoside extend into the solvent. O‐2 is hydrogen‐bonded through a water molecule to an adjacent asymmetric unit. O‐1 is not involved in any hydrogen bond and there is no fixed position for its methyl substituent.