A theoretical framework is presented to clarify the role of architectural and structural forces in ion selectivity. It expresses the relative free energy of bound ions in terms of a reduced subsystem corresponding to the local degrees of freedom coupled to the rest of the protein. The latter is separated into a first contribution that includes all the forces keeping the ion and the coordinating ligands confined to a microscopic sub-volume but do not prevent the ligands from adapting to a smaller ion, while the second contribution regroups the remaining forces that serve to dictate the precise geometry of the coordinating ligands best adapted to a given ion. The theoretical framework makes it possible to delineate two important limiting cases. In the limit where the geometric forces are dominant (rigid binding site), selectivity is controlled via the cavity size according to the familiar “snug-fit” mechanism of host-guest chemistry. In the limit where the geometric forces are negligible, the ion and ligands behave as a dynamical “confined droplet” that is free and adapt to the ion’s size. In this case, selectivity is controlled by the number and the chemical type of ion-coordinating ligands.