Histone methylation reader proteins (HMRPs) regulate gene transcription by recognizing, at their "aromatic cage" domains, various Lys/Arg methylation states on histone tails. Because epigenetic dysregulation underlies a wide range of diseases, HMRPs have become attractive drug targets. However, structure-based efforts in targeting them are still in their infancy. Structural information from functionally unrelated aromatic-cage-containing proteins (ACCPs) and their cocrystallized ligands could be a good starting point. In this light, we mined the Protein Data Bank to retrieve the structures of ACCPs in complex with cationic peptidic/small-molecule ligands. Our analysis revealed that the vast majority of retrieved ACCPs belong to three classes: transcription regulators (chiefly HMRPs), signaling proteins, and hydrolases. Although acyclic (and monocyclic) amines and quats are the typical cation-binding functional groups found in HMRP small-molecule inhibitors, numerous atypical cationic groups were identified in non-HMRP inhibitors, which could serve as potential bioisosteres to methylated Lys/Arg on histone tails. Also, as HMRPs are involved in protein-protein interactions, they possess large binding sites, and thus, their selective inhibition might only be achieved by large and more flexible (beyond rule of five) ligands. Hence, the ligands of the collected dataset represent suitable versatile templates for further elaboration into potent and selective HMRP inhibitors.