Fig. 4: Structure of CxD7L1 in complex with ADP. | Nature Communications

Fig. 4: Structure of CxD7L1 in complex with ADP.

From: ADP binding by the Culex quinquefasciatus mosquito D7 salivary protein enhances blood feeding on mammals

Fig. 4

a Ribbon representation of CxD7L1-ADP structure. The 17 α-helices are labeled A–Q. b Several views of CxD7L1 differing by rotations of 90° around the y-axis. N-terminal and C-terminal are colored in blue and green, respectively. ADP is shown as a stick model in magenta and disulfide bonds in orange. c Electron density map covering ADP. CxD7L1 protein is colored in green. d Inset from (c) is shown. Amino acid residues of CxD7L1 involved in ADP binding are colored in green (e). Stereo view of the binding pocket of the CxD7L1-ADP complex showing the 2Fo − Fc electron density contoured at 1σ covering the ligand. All residues within a 3.6 Å distance from the ADP are shown. Hydrogen bonds are colored in yellow. GOL-402 is a glycerol molecule that is in the area of the phosphate group. R271 was not included in the figure as it is not within 3.6 Å and it binds N265, but it does not bind ADP directly.

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