Fig. 2
From: The molecular basis of phosphite and hypophosphite recognition by ABC-transporters
A detailed comparison of the spatial arrangement of the binding pocket and network of interactions around the ligand. The interior surface (partially transparent, atom colours) of the binding pocket and surrounding residues (sticks) in a Te_PtxB; b Pm_PhnD; c HtxB and d E. coli PhnD (PDB:3P7I). In each case, the capping residues are highlighted with a dotted surface that represents the van der Waals radii of the atoms. The external surface is also shown in each case, demonstrating how the binding pocket in reduced phosphorus binding PBPs (a–c) is buried from the external solvent and in each case is much smaller than that of the phosphonate binding PhnD from E. coli (d). The protein backbone is drawn as a cartoon, with sidechains drawn in sticks and hydrogen bonds between the capping residues indicated by black dashes. Each figure (a–d) is accompanied by a schematic (e-h) that displays the hydrogen-bonding network between the protein and the oxygen atoms of the ligand. The 2-aminoethyl group of 2AEPn is abbreviated to 2AE in h
