Fig. 4: AtPFA-DSP1 binds 5-PP-InsP4 in two orientations, which are associated with either the presence or absence of Pi. | Nature Communications

Fig. 4: AtPFA-DSP1 binds 5-PP-InsP4 in two orientations, which are associated with either the presence or absence of Pi.

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

Fig. 4

Panels (a, b) are surface representations of the ligand binding pocket, with 5-PP-InsP4 drawn in stick format, in poses labeled β-IN (pale lavender carbons) and β-OUT (green carbons), respectively; phosphorus is orange and oxygens are red. Note the presence of Pi(B) (in stick and ball format) in panel (b). Panels (c, d) show the corresponding stick depictions of 5-PP-InsP4 and its interacting amino-acid residues (nitrogens are colored blue). The Fo-Fc electron density maps (green mesh) are contoured at 3σ in panel (c) and 5σ in panel (d). Panels (e, f) are renderings of the corresponding ligand–protein interactions created by Ligplot+. The source data file is provided as PDB accession code 7MOH.

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