Several conformations of the viral s-glycoprotein have been observed by electron microscopy, including both semi-open (PDB ID 6VYB) and closed (PDB ID 6VXX) conformations. The existence of visibly different conformations demonstrates that the viral s-glycoprotein can undergo conformational changes affecting not just its surface but also the gorge within the S1 subunit and the S2 subunit. Because most studies have focused on localised sites such as the active site of the viral Mpro protease or the receptor-binding domain of the s-glycoprotein, we felt that there was a gap in our knowledge about the virus and that several steps along the pathway from infection to propagation remain to be explored. In particular, the long putative tunnel created by the formation of the s-glycoprotein trimer has, to our knowledge, received little study. Studying drug interactions in such long tunnels would be laborious and computationally expensive if using alchemical or ligand migration methods. However, a long tunnel is a perfect target for study with CaverDock. CaverDock is an in-house tool that uses Caver, to identify tunnels in protein structures, and an optimised version of the well-established algorithm from AutoDock Vina to calculate possible ligand trajectories along those tunnels and the corresponding binding energies. CaverDock discretises each identified tunnel into a series of discs and models a ligand's passage through the tunnel by constraining one ligand atom to lie within a disc a time, sequentially. The ligand's conformation and binding energies are then calculated using Autodock Vina, with the ligand (aside from the constrained atom) being free to explore the conformational space; the protein is treated as a rigid body. Once the conformation and binding energy have been calculated, the constrained atom is shifted to the next disc and the process is repeated until the ligand has moved through the full length of the tunnel. The tool is continuously maintained and is freely available as both a stand-alone program and a webtool named CaverWeb. Since the start of the pandemic, the scientific community has recognized the need for collaboration and sharing of results by pledging to make data publicly available as soon as possible. In this work, we used data from a 10 µs molecular dynamics (MD) simulation of the s-glycoprotein trimer conducted at the D.E. Shaw Institute, from which we extracted the main representative conformations.