Cation-π interaction is a non-covalent binding force that plays a significant role in protein stability and drug-receptor interactions. In this work, we have investigated the structural role of cation-π interactions in sugar-binding proteins (SBPs). We observed 212 cation-π interactions in 53 proteins out of 59 SBPs in dataset. There is an average one energetically significant cation-π interaction for every 66 residues in SBPs. In addition, Arg is highly preferred to form cation-π interactions, and the average energy of Arg-Trp is high among six pairs. Long-range interactions are predominant in the analyzed cation-π interactions. Comparatively, all interaction pairs favor to accommodate in strand conformations. The analysis of solvent accessible area indicates that most of the aromatic residues are found on buried or partially buried whereas cationic residues were found mostly on the exposed regions of protein. The cation-π interactions forming residues were found that around 43% of cation-π residues had highly conserved with the conservation score ≥6. Almost cationic and π-residues equally share in the stabilization center. Sugar-binding site analysis in available complexes showed that the frequency of Trp and Arg is high, suggesting the potential role of these two residues in the interactions between proteins and sugar molecules. Our observations in this study could help to further understand the structural stability of SBPs.