Discrete three-dimensional (3D) organic and metal-organic (porous) cages have emerged as promising biomimetic systems. They offer synthetic modularity and tunability, enabling chemists to efficiently create structures with customized sizes and shapes from simple building blocks. A critical factor contributing to their functional properties is the presence of a welldefined inner cavity capable of binding and even catalyzing chemical reactions, prompting chemists to draw parallels between these systems and enzymes. In molecular cages, the affinity of the host towards a particular guest depends on various structural and electronic parameters. A key structural parameter used to assess the ability of a cage to act as a host is the relative cavity size of the cage and guest molecules. For instance, Rebek determined that 'closed' organic capsules exhibit binding when the guest occupies around 55% of the host cavity volume. Since then, this rule has been extended to other supramolecular structures with varying success, and also to enzymes. Several tools have been developed for the identification and characterization of protein binding pockets based on grid, rolling probe, or tessellation algorithms, including VOIDOO, McVol, Volarea, GRASP, CAVER, CAST, HOLLOW, MDpocket, ProteinVolume, 3V, Voronoia, PoreBlazer, Zeo++, and CavVis. However, most of these cannot be easily adapted for supramolecular cages, and software exclusively dedicated to cage architectures is scarce, with PyWindow, and MoloVol being the only notable examples.