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. 2005 Jun 17;102(26):9144–9149. doi: 10.1073/pnas.0502082102

Fig. 4.

Fig. 4.

Active site of yPNGase and the surface representation of the yPNGase-yRad23XBD complex. (A) Interactions between yPNGase and the inhibitor (Left) or sucrose molecules (Center and Right). A sucrose molecule in site 1 of yPNGase (Center) is replaced by an inhibitor, Z-VAD-fmk, but the other two sucrose molecules in sites 2 and 3 remained in the same position upon inhibitor binding (Right). H-bonds are represented by dashed lines. O, N, and S atoms are shown in red, blue, and orange, respectively. Residues that replaced in mutational analyses are marked with red circles. (B) The molecular surfaces of yPNGase and yRad23XBD are colored in white and yellow, respectively. The surface of the yPNGase residues that is >80% conserved in four yPNGase orthologues (Fig. 2) is colored in purple. A catalytic triad is shown in yellow. Axes indicate the close-up views for the inhibitor and sugar-binding sites.