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Figure 4.
Figure 4. Structural comparison of the active sites of EFEa
and its closely related serine proteases based on their global
C^a superposition. The superposition of some important active
site residues is shown, including the catalytic triad and the
substrate-discriminating residues (189, 226 and 216) in the S1
specificity pockets of EFEa (in yellow) and (a) tPA[50] (PDB
code: 1BDA); (b) chymotrypsin (1DLK); (c) HLE (1PPG) and (d) PPE
(4EST) (all in maroon). The specific inhibitors (in green) bound
to the various enzymes were introduced into the active site of
EFEa to demonstrate the fitting of the P1 residues. Identical
residues are labeled in black, while different ones are labeled
with their corresponding colors. For clarity, only the P1-P3
residues are drawn for the inhibitors.
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