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Figure 5.
Fig. 5. (A) Fluorine interacts favorably with peptidic N–H
(ligand Cs in green) and C=O (ligand Cs in purple) moieties. (B)
Fluorine undergoes dipolar interactions with side-chain amides
of Gln and Asp (ligand Cs in yellow). (C) The C–F residue of a
tricyclic inhibitor undergoes a multipolar interaction with the
backbone C=O of Asn98 in the D pocket of thrombin (table S1,
entry 23). (D) A dipolar N–H···F–C
interaction induces the shown conformation of a thrombin
inhibitor within the enzyme (fig. S3 and table S1, entry 22).
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