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. 2016 Dec 28;11(12):e0168485. doi: 10.1371/journal.pone.0168485

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© 2016 Christensen et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 5 — Surface representation for CtDsbA of the catalytic (left) and non-catalytic (right) faces. The active site residues Cys-Ser-Ala-Cys are colored yellow and the nucleophilic cysteine sulfur highlighted in orange. Pockets formed on the posterior face of the protein between H1 and H3 (pocket 1) and the N-terminal unstructured region and H6 (pocket 2) are labeled. B. Electrostatic surface representation of CtDsbA. Views are oriented as above. Electrostatic surface potential is contoured between -5 (red) and +5 (blue) kT/e. The nucleophilic cysteine is annotated with an S.