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Figure 5.
Figure 5 Superposition of bovine trypsin (I) and Daiichi's
DX-9065a (PDB entry 1mtw) complexes. The C atoms of the
inhibitor (I) and DX-9065a are colored green and blue,
respectively. The majority of the C atoms in the trypsin bound
to (I) are gray and those bound to DX-9065a are black. C atoms
of specific residues have been colored. Asp189 (177) at the
bottom of the S1 pocket is colored light blue. The catalytic
triad Ser195 (183), His57 (46) and Asp102 (90), are colored
orange. Residues which form the S4 pocket, Thr98 (86), Leu99
(87), Gln175 (161) and Trp215 (199), are colored purple.
Hydrogen bonds are depicted as dashed lines. Hydrogen bonds to
the naphthylamidine in DX-9065a have been omitted for clarity,
as they are identical in both complexes.
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