GPRs are responsible for a variety of biological functions, and design of small molecule antagonists for GPRs is of interest in the field of computational drug design. The structure and dynamics of the side binding pocket of the GPR101-Gs complex (PDB: 8W8R) have been shown to influence binding in computational antagonist design. The structure of the GPR101-Gs protein was obtained from the PDB (PDB: 8W8R) and truncated to the side binding pocket of GPR101. Water molecules and ions were removed from the structure to allow space for the molecular probe. Multiple conformations of these proteins were not considered to reduce computational cost, but in principle this workflow could be applied to analyze pockets changes across conformational ensembles.