Fig. 2: Description of the Pi(A) orientation associated with crystals of freshly purified AtPFA-DSP149–215 and AtPFA-DSP149–150,C150S,151–215. | Nature Communications

Fig. 2: Description of the Pi(A) orientation associated with crystals of freshly purified AtPFA-DSP149–215 and AtPFA-DSP149–150,C150S,151–215.

From: A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop

Fig. 2

Panels (a, b), show the phosphate ion in stick and ball format (phosphorus is orange and oxygen in red) within a mixed stick- and ribbon-style rendition of the catalytic center of wild type and the C150S protein constructs, respectively (nitrogen is blue, sulfur is yellow). The omit Fo-Fc electron density maps, contoured at 5σ, are shown in green mesh; broken black lines show polar contacts. Corresponding ligand–protein interactions created by Ligplot+ are shown below each graphic. Source data are provided for (a, b) as PDB accession codes 7MOK and 7MOD, respectively.

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