Molecular interactions between setron and 5-HT3AR in 5-HT3AR-Grani, 5-HT3AR-Palono, 5-HT3AR-Ondan, 5-HT3AR-Alo and between serotonin and 5-HT3AR in 5-HT3AR-Serotonin structures during MD simulation. 5-HT3AR-setron interaction fingerprints were derived for each ligand-protein complex by averaging across each protomer chain from 100 ns MD simulations. Interactions were assessed between ligand and protein and reported for those that had an average probability above 10%. Nine interaction types were calculated: apolar (hydrophobic), face-to-face aromatic (Aro_F2F), edge-to-face aromatic (Aro_E2F), hydrogen bond with the protein as hydrogen-bond donor (Hbond_ProD), hydrogen bond with the protein as hydrogen- bond acceptor (Hbond_ProA), electrostatic with the protein positively charged (Elec_ProP), electrostatic with the protein negatively charged (Elec_ProN), one-water-mediated and two-water-mediated hydrogen-bond interactions (Hbond_1Wat and Hbond_2Wat). Electrostatic interactions with positively charged protein residues (Elec_ProP) were not found in any of our studied setron-bound 5-HT3AR simulations.