[Objectives]  To obtain the three-dimensional structure of the odorant binding protein (OBP) of the red palm weevil, Rhynchophorus ferrugineus, a notorious invasive pest, in order to develop potential volatile compounds to control this weevil based on the computational reverse chemical ecology approach. [Methods]  Two, three dimensional structures of R. ferrugineus were homologically modeled based on crystal structures of OBPs from other insects that have been deposited in the Protein Data Bank (PDB). The modeled structures were evaluated by Procheck, VERIFY_3D and ERRAT and their evaluation scores indicate that model quality is high. [Results]  The two, modeled, putative, three-dimensional, R. ferrugineus OBPs were composed of 6 α helixes and rebounds connecting the helixes. Three pairs of disulfide bonds formed by 6 cysteines were the key to their structural stability. [Conclusion]  These modeled OBP structures lay a foundation for the future screening of potential active volatiles to control R. ferrugineus by molecular docking.