## 4 Discussion
In the current study, we initially performed protein-protein docking of the S-protein and the TIM-1 receptor, and docking sites were noted (Figure 3). We found that the S-protein interacted with the TIM-1 protein through 11 different residues (Table 2). However, among those 11 residues, Lys56, Arg54, and Val181 were the residues that were previously known to be significant for viral entry into the cell. These results confirm the finding of previous studies [33; 34; 35; 36; 37]. In the next step, Lumateperone was docked with the S-protein. The S-protein/Lumateperone docked complex interacted through five different residues (Table 2); between them, two residues, i.e., Ala459 and Asn461, were the residues of the highly glycosylated mucin-like domain of the S-protein (MCD). The MCD domain is from 313-464 on the S-protein [37]. Previously, it has been documented that a major function of the MCD domain is to protect the glycoproteins from cell surface proteolysis and also protect the cells from attack by other cells [38]. From these results, we can presume that binding Lumateperone to the residues of the MCD domain of the S-protein may affect the efficiency of viral entry and also lessen the viral protective core. In the case of the TIM-1/Lumateperone docked complex, TIM-1 and Lumateperone interacted through 11 different residues as shown in Table 2. Between them, two residues, i.e., Asn461 and Trp274, were the common residues that were also involved in the interaction with the S-protein during the S-protein/TIM-1 docked complex formation (Figure 3). These results also indicate that Lumateperone could be a possible inhibitor of S-protein/TIM-1 docking. Furthermore, we then docked Lumateperone with the S-protein and then docked that complex with the TIM-1 receptor. Similarly, in the next step, we docked Lumateperone first with the TIM-1 receptor, and then that complex was docked with the S-protein. In this way, we obtained two different complexes. In the first, Lumateperone was initially docked with the S-protein. In the second, Lumateperone was initially docked with the TIM-1 receptor as shown in Figure 5. We found that in both the complexes, Lumateperone decreased the binding energies of the S-protein/TIM-1 complex. Lumateperone was docked either with the S-protein or the TIM-1 receptor before complex formation (Figures 4 and 5). Moreover, we knew that the lower the binding energy, the more unstable the complex would be [39]. So, we obtained a more unstable complex in the case where Lumateperone was bound either to the S-protein or the TIM-1 receptor in the complex. Not only did the bind energies of the complexes decrease, but the interaction between the S-protein and the TIM-1 protein also decreased in terms of interacting residues, the position of the interacting residues, and the bonding of interacting residues as in Table 3.  
From various evidence, the results attained in this study showed that Lumateperone binds mostly to the region of the S-protein which is vital in binding with host cell [40]. Moreover, it was observed that Lumateperone binds to the TIM-1 at sites which served as a medium for virus entrance, i.e., Lys56, Arg54, and Val181 [37; 40]. Therefore, outcomes of the current computational study propose that the use of Lumateperone prevents virus infection. It is obvious from the computational study arrangement that blocking the attachment of the host cell receptors to the virus by this inhibition mechanism and the inhibition of the virus protein cellular entrance might be an effective therapeutic target. However, this needs to be experimentally validated prior to translational intervention. Hence, in the host system, the availability of Lumateperone may facilitate various mechanisms at the same time and thus promote removal and/or neutralization of virus infection.