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Figure 7.
Fig. 7. a: Structure and (2|F[o]|−|F[c]|), α[c] map of
trypsin–APC-11922, 1.50 Å resolution. For the major
inhibitor conformer (opaque sticks) there is a hydrogen bond
between the inhibitor phenol (O6′) and Nε2[His57], and a
short O6′–Oγ[Ser195] hydrogen bond. b: Structure and
(2|F[o]|−|F[c]|), α[c] map of uPA–APC-11421, 1.75 Å
resolution. In this and all other uPA complexes of the APC-7136
analogs in Fig. 2b, the phenol hydroxyl is at or near the
oxyanion hole, receiving hydrogen bonds from N[Gly193] and from
the inhibitor NH amide group. In many trypsin and thrombin
complexes the inhibitor is discretely disordered between the two
binding modes in (a) and (b).
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