The presented study analyzed potential binding sites of 3,5,4'-trihydtoxystilbene (resveratrol, RSV) and its derivative, trans-3,3', 5,5'-tetrahydroxy-4'-methoxystilbe (THMS) to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The effects of stilbene analogs, on the structure of GAPDH were determined by fluorescence spectroscopy and zeta potential measurements. To what extent the studied compounds affect the activity of the enzyme was also assessed. A-computational ligand-docking study showed that there are 11 potential binding sites of RSV and 8 such sites of THMS in the GAPDH molecule. While resveratrol does not significantly affect the activity of the dehydrogenase upon binding to it, THMS, leads to approximately 10% inactivation of this enzyme. THMS has no effect on GAPDH inactivation induced by the superoxide anion radical, in contrast to resveratrol, which increases dehydrogenase inactivation.