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Figure 3.
Fig. 3. Primary and secondary binding. Stereo plot of the primary and secondary binding of the BPTI (blue) to anionic salmon trypsin (red). The
N
#
atom of P1 lysine contacts the carboxylate group of Asp189 through one direct hydrogen bond to O
#2
and through a water molecule to O
#1
. Five
hydrogen bonds, which all contact the inhibitor main chain, are conserved in the secondary binding sites of all three complexes. Two are on the N
terminal side of the scissile bond, and three on the Cterminal side. Additional hydrogen bonds are formed between inhibitor side chains and the
enyme (see Table 4 for further details). The figure was prepared using BOBSCRIPT [33, 34].
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