Colchicine derivatives are currently under scrutiny as potential candidates for future cancer therapeutic applications, leveraging the well-established antimitotic properties of colchicine. In this study, a comprehensive computational model of the colchicine binding site has been constructed within tubulin heterodimers. To achieve this, AlphaFold2 has been employed to generate three-dimensional structures of human beta tubulin in its wildtype and mutated form. A human alpha tubulin structure from available data bank online has been used to create the heterodimer, subsequently modifying the geometry of the heterodimer incorporating colchicine. This homology modeling approach was guided by crystallographic data from colchicine-docked microtubules in bovine cells.