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. Author manuscript; available in PMC: 2016 Mar 1.
Published in final edited form as: Free Radic Biol Med. 2014 Aug 1;0:171–182. doi: 10.1016/j.freeradbiomed.2014.07.037

Figure 2.

Figure 2

Structure of human PDI. The coordinates for the oxidized protein are from Wang et al. [28]. Redox-active CxxC motifs are found in both a and a′ domains. The N-terminal cysteine sulfur atom of each motif (orange) is solvent accessible and engages in mixed disulfides with redox partners and proteins undergoing disulfide editing. The C-terminal cysteine by contrast is largely buried from solvent (yellow). The b and b′ domains are redox-inactive. Protein clients of PDI can occupy the central cavity with significant hydrophobic interactions with the b′ domain.