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C32 is the second active-site cysteinyl residue of PfGrx and C88 is the third cysteinyl residue, which is in the proximity of the active site and can also undergo redox modifications 14,26,30

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Moreover, the greater stability of the Cagri-induced bypass conformation relative to the rAmy-induced bypass conformation, when engaged with the CTR, is likely a major contributor to the increased conformational stability of the Cagri-AMY 2 R-Gs complex relative to the rAmy-AMY 2 R-Gs complex

Journal of Neurosurgery 76(1):72-80