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. 2016 Oct 10;55(45):13985–13989. doi: 10.1002/anie.201606449

Figure 2.

Figure 2

Analysis of the conformational and binding properties of MCs by inspection of several phosphatase–ligand complexes. A) The presence of a molecule of water (ball and stick model) in a pocket close to the metal ions (pale purple spheres) in PP1 (PDB ID: 3HVQ). B) An overlay of two PP1 crystal structures, one co‐crystallized with MC (stick model; PDB ID: 2BDX) and the other with a water molecule in the hydrophobic groove (ball and stick model; PDB ID: 3HVQ). C) Alignment of crystal structures of PP1 (C atoms white) and PP2A (C atoms gray), showing a possible hydrogen bond between a carbonyl group of MC and Arg268 of PP2A (MC extracted from PDB ID 3FGA and merged into PP2A of PDB ID 4I5L). This H‐bonding is not possible in PP1 (PDB ID: 2BDX) as it has a Glu at the corresponding position. D) An alignment of Phe276 (PP1, PDB ID: 2BCD) and Cys269 (PP2A, PDB ID 2IE4), shown as ball and stick models, with the protein backbones shown as ribbon diagrams, and lines showing dihydro‐MC‐LA.