Our research is focused on bacterial lectin RS20L from Ralstonia solanacearum.The RS20L lectin displays a different structure from these two, and no structure homologue was found for this lectin in the bacterial lectin realm. Its fold resembles animal realm galectins. The native lectin structure was crystallized, and during the experimental preparation of a recombinant form and attempts of functional characterization, several cases of very peculiar behavior were recorded extremely high stability of trimeric form, irreversible loss of binding properties after purification, etc. The research focuses on investigating the general and binding properties of the RS20L lectin that could help to explain this unusual behaviour. The study was performed by means of computational chemistry and molecular modelling. Several promising hints were found that could, upon further investigation, help to decrypt the reasons behind the lectin behavior.