ADP/ATP translocase is very specifically inhibited by two families of compounds. The first family, which includes atractyloside (ATR) and carboxyatractyloside (CATR), binds to the ADP/ATP translocase from the cytoplasmic side, locking it in a cytoplasmic side open conformation. In contrast, the second family, which includes bongkrekic acid (BA) and isobongkrekic acid (isoBA), binds the translocase from the matrix, locking it in a matrix side open conformation. The negatively charged groups of the inhibitors bind strongly to the positively charged residues deep within the binding pocket. The high affinity (K in the nanomolar range) makes each inhibitor a deadly poison by obstructing cellular respiration/energy transfer to the rest of the cell. There are structures available that show the translocator locked in a cytoplasmic state by the inhibitor carboxyatractyloside, or in the matrix state by the inhibitor bongkrekic acid.