Figure 6: Modelling of C-terminal residues of Ce-2 onto Ce-2d. | Nature Communications

Figure 6: Modelling of C-terminal residues of Ce-2 onto Ce-2d.

From: Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases

Figure 6

(a) The Ce-2d macrocycle is shown as worm α-chain (gold) representation scaled by B-factor within a cavity of C. elegans iPGM residues (transparent spheres) formed from residues within 5Å of cyclic peptide. The C-terminal residues, -Gly12-Thr13-Cys14-Gly15 of Ce-2 were modelled onto the iPGM·Ce-2d complex and are shown as tan sticks extending from Ce-2d. Electrostatic surface of the binding cavity is also shown. (b) Ce-2 van der Waals radii shown using a CPK model. The Cys14 sulfhydryl is shown in yellow.

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