The binding pocket is lined by several aromatic residues, many of which are conserved amongst pLGICs. These residues form an "aromatic cage" which helps pockets recognise ligands and stabilise ligand binding through cation-π interactions, besides hydrogen bonds. Upon glycine binding, across all models of our simulation, about two cation-π interactions are formed. The most important aromatic residue, in this context, is PHE175 (in Loop B) which forms cation-π interactions with a high occurrence (over 97 %,) as well as participating as donor in hydrogen bonding (with varying occurrence ranging from 11 to 66 %). TYR218 and PHE223 (in Loop C) and PHE79 (in Loop D) can also participate in cation-π interactions, although less frequently (with varying occurrence in the range of 16-87%, 30-60%, and 1-16%, respectively).