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Figure 1.
Figure 1. The electron density for the P1 residue of BPTI
and residues Ser189, Ser190 and Met192 of chymotrypsin together
with the hydrogen bonding pattern of the P1 side-chain in the
structures of the following complexes: (a) Chtp-K15E BPTI; (b)
Chtp-K15M BPTI; (c) Chtp-K15H BPTI; (d) Chtp-K15T BPTI; (e)
Chtp-K15W BPTI. The 2F[o] -F[c] maps were contoured at 1.5s.
Selected side-chains are indicated in red, the binding loop of
the inhibitor in orange and the S1 binding pocket of the enzyme
in gray (only the main-chain of the S1 pocket together with
Cys191 and Cys220 side-chains is presented for clarity). This
and the following Figures were produced with the program
XtalView.47
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