Proteasomes play a key role in maintaining protein homeostasis in mammalian cells and protozoan parasites alike. Human parasites such as Trichomonas vaginalis (Tv) with their 20S proteasomes are recognized as viable drug targets. In insect cells we have recombinantly expressed of all fourteen proteins of the Tv20S proteasome, containing seven α and seven β subunits with coexpression of the Ump-1 proteasome chaperone. The purified Tv20S was successfully enzymatically active, and subsequent enzymatic assays have reviealed that Tv20S is a viable target for inhibition by the natural product marizomib (MZB) and peptide inhibitor carmaphycin-17 (CP-17). We conducted Negative stain analysis and Cryo-electron microscopy (cryo-EM) and elucidated two Tv20S cryo-EM structures one with MZB and the other with CP-17 inhibitors. The final resolutions was 2.6е, and 2.86 е respectively. Overall this study outlines the binding details of MZB and CP-17 and provides valuable insights into the possible targetting of Tv20S over human proteasome. The data unveil promising avenues for exploiting these binding sites in future drug design and developments.