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Figure 4.
Figure 4. Stereo view showing a superposition of the active
sites of the E2 complex (a), and E2* complex (b), onto the ES
complex. Carbon atoms of the active-site residues in the ES
complex are colored grey, while those in the tetrapeptide
substrate are colored black. The E2, E2*, and model tetrahedral
intermediate complexes are shown with yellow carbon atoms in the
protein residues and orange in compound 2. Notice the similarity
between the conformations of the substrate and inhibitor,
especially the region near the catalytic Ser62. The rmsd between
E2 and ES is 0.22 Å, while that of the E2* and ES
structures is 0.31 Å, for all atoms in the 16 active-site
residues. In (c) the E2 structure is overlaid on an
energy-minimized model of the tetrahedral intermediate with
peptide substrate. The Figure was produced using MOLSCRIPT.39
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