Initially, these domains are parallel when the channel is in a closed state, maintaining a structured configuration. However, the scenario changes post a 200ns molecular dynamics (MD) simulation, where a noticeable twist in the domains is observed as shown in Figure . This twist is indicative of structural transformations happening within the ion transport process of the channel, embodying a dynamic mechanism. The structural metamorphosis doesn't just stop at domain twisting; it further manifests in the outward displacement of the residues E8 and N15. This outward migration is not arbitrary but is in line with the findings of experimental studies. These studies conjecture a significant role for E8 and N15 residues when the ion channel is in a closed state. They seem to bind to the metal ion, setting the stage for the ion's accommodation and subsequent transport. This preparation is crucial for the ion transport process, ensuring the ions are in the right position before the actual transport occurs. The once accommodating E8 and N15 residues distance themselves, letting go of the ion. This release is not haphazard but seems to be a calculated move, dropping the ion precisely towards the channel opening. This mechanism underscores a wellcoordinated sequence of events that regulate ion transport through the channel, showcasing a blend of structural and functional intricacies inherent in the ion channel dynamics. The twisting motion led to the outward movement of residues F20, F23, and F26, resulting in a change in hydrogen bonding among these residues as shown in Figure . This phenomenon has been confirmed in experimental studies. As a result, it can be concluded that Phe residues in the open state do not obstruct the channel pore. Silva et al. have proposed that the structural changes in the N and C termini facilitate ion permeation through a specific mechanism. According to them, the "Phe" motif located between amino acid residues 20 and 26 serves as a signaling relay system for conformational changes by influencing the orientations of the aromatic side chains. Furthermore, 19F NMR studies have shown that both F20 and F26 can adopt two distinct side-chain conformations, which affect their exposure to lipids and water. These findings imply that the equilibrium between the conformations of F20 and F26 may impact the channel's pore diameter and the overall structural stability of the helical bundle.