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. 2014 Apr 16;289(22):15527–15535. doi: 10.1074/jbc.M114.564278

FIGURE 3.

FIGURE 3.

Positioning of key active site residues in the EcLpxA-RJPXD33 complex. A, the 2Fo − Fc electron density map of the RJPXD33-LpxA complex contoured to 1σ around RJPXD33 (cyan; stick) with amino acids from LpxA (gray; stick) that surround the bound ligand. Although the full density of the methionine side chain from RJPXD33 could not be visualized, His-160 of LpxA kinks away from the hydrophobic cleft, allowing space for the methionine side chain to occupy the binding pocket. B, close-up overlay stereo view of the EcLpxA-RJPXD33 complex (PDB code 4J09; enzyme (gray); RJPXD33 (cyan)) and EcLpxA (PDB code 1LXA; green) with no bound ligands. PyMOL alignment r.m.s.d. = 0.35 over 256 residues.