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Figure 3.
Figure 3. (a) Structure of
uPA–thieno[2,3-b]pyridine-2-carboxamidine, pH 6.5, at 1.65
Å resolution, on the (2|F[o]|–|F[c]|), α[c] map. The
occupancies of conformation 1 (with green carbons) and 2 (light
green carbons) are 66% and 34%, respectively. In the trypsin
complex the corresponding occupancies are 54% and 46% at pH 5.5,
and 31% and 69% at pH 8.2. (b) Superposition of uPA– and
trypsin–thieno[2,3-b]pyridine-2-carboxamidine, pH 5.5. For
clarity only the first conformation of the bound inhibitors is
shown. In each complex the aromatic rings of the two bound
conformations of the inhibitors lie in the same plane as one
another (see Figure 4a). The two locations of the Hγ proton of
Ser195 for the trypsin complex are shown.
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