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. 2019 Mar 28;116(16):8048–8053. doi: 10.1073/pnas.1820639116

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Fig. 4. — Active-site and TRX-dependent regulation of CrPRK. (A) The catalytic cavity is shown. The distance between the regulatory cysteines is greater than 13 Å. (B) The electrostatic surface potential of the catalytic cavity is shown. The bottom of the catalytic cavity is marked by a positive potential. The negative potential observed in the left side of the cavity is thought to be involved in the correct positioning of TRX close to the regulatory cysteines. (C) The pK_a of Cys16 was determined by measuring the IAM-mediated inactivation as a function of pH. (D) The molecular environment of Cys16, considering a sphere of 5 Å centered on its thiol group. The hydrogen bonds between the thiol group and the neighboring residues and the corresponding distances are shown.