Drug efficacy often correlates better with dissociation kinetics than binding affinity alone. To study binding kinetics computationally, it is necessary to identify all of the possible ligand dissociation pathways. The site identification by ligand competitive saturation (SILCS) method involves the precomputation of a set of maps (FragMaps), which describe the free energy landscapes of typical chemical functionalities in and around a target protein or RNA. In the current work, we present and implement a method to use SILCS to identify ligand dissociation pathways, termed "SILCS-Pathway." The A* pathfinding algorithm is utilized to enumerate ligand dissociation pathways between the ligand binding site and the surrounding bulk solvent environment defined on evenly spaced points around the protein based on a Fibonacci lattice. The cost function for the A* algorithm is calculated using the SILCS exclusion maps and the SILCS grid free energy scores, thereby identifying paths that account for local protein flexibility and potential favorable interactions with the ligand. By traversing all evenly distributed bulk solvent points around the protein, we located all possible dissociation pathways and clustered them to identify general ligand unbinding pathways. The procedure is verified by using proteins studied previously with enhanced sampling molecular dynamics (MD) techniques and is shown to be capable of capturing important ligand dissociation routes in a highly computationally efficient manner. The identified pathways will act as the foundation for determining ligand dissociation kinetics using SILCS free energy profiles, which will be described in a subsequent article.