We have recently demonstrated that certain oligomannose and bisected hybrid-type glycopeptides are bivalent for concanavalin A (ConA) binding and that they can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzoni, P & Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293]. Two protein-binding sites on each glycopeptide were identified: one on the alpha(1-6) arm of the core beta-mannose residue which binds with high affinity (primary site); the other on the alpha(1-3) arm of the core beta-mannose residue which binds with lower affinity (secondary site). In the present study, we have investigated the relationship between the structures of the primary sites of oligomannose-type glycopeptides and their affinities for ConA. Two mechanisms of binding at the primary sites of oligomannose-type glycopeptides have been identified which account for the 3000-fold increase in affinity of a Man9 glycopeptide relative to that of methyl alpha-D-mannopyranoside. Changes in the structures and affinities of both the primary and secondary sites are observed to influence the precipitation activities of the glycopeptides. These findings have important consequences for the specificity of ConA binding in solutions containing mixtures of the carbohydrates.