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. Author manuscript; available in PMC: 2016 Dec 1.

Published in final edited form as: Biochim Biophys Acta. 2015 Sep 3;1854(12):1809–1815. doi: 10.1016/j.bbapap.2015.09.001

The structure of pPAF-AH complexed with soman (9). Panel A shows a space-filled, partially cut-down structure of pPAF-AH with soman adducted to S273 and shows the residues surrounding the active site S273 and H351. F322, W298 and L153 are sites for mutagenesis. Panel B shows the approximate angle (yellow arc) and distance (red line) to the S273 O^γ for F322 if we assume S273 is the vertex and the direction to the active site histidine (H351) forms one side (red line). F322 is closest to S273 O^γ at 4.8 Å and sits close to H351 at approximately 44°. Panel C shows L153 is offset from H351 by approximately 121°, but it is more than 5.8 Å away from S273 O^γ. Panel D shows W298 offset from H351 by approximately 126°, and at a position of 6.7 Å from S273 O^γ.

The structure of pPAF-AH complexed with soman (9). Panel A shows a space-filled, partially cut-down structure of pPAF-AH with soman adducted to S273 and shows the residues surrounding the active site S273 and H351. F322, W298 and L153 are sites for mutagenesis. Panel B shows the approximate angle (yellow arc) and distance (red line) to the S273 O^γ for F322 if we assume S273 is the vertex and the direction to the active site histidine (H351) forms one side (red line). F322 is closest to S273 O^γ at 4.8 Å and sits close to H351 at approximately 44°. Panel C shows L153 is offset from H351 by approximately 121°, but it is more than 5.8 Å away from S273 O^γ. Panel D shows W298 offset from H351 by approximately 126°, and at a position of 6.7 Å from S273 O^γ.