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Figure 4.
Figure 4. Differences between the complex structures of WT and
GPLGS-WT. (a) Inhibitor N3. (b) Superposition of the
substrate-binding pockets in protomer A of GPLGS-WT and that in
protomer A* of WT. In the WT-N3 complex structure, the NH[2]
group of Ser1 in protomer B* was still hydrogen-bonded to the
carboxylate group of Glu166 and the carbonyl group of Phe140 in
protomer A*, stabilizing the S1 pocket. In the GPLGS-WT-N3
complex structure, however, the two hydrogen bonds described
above were not found. Instead, an ordered water molecule was
observed in the S1 pocket. Protomer A* of WT is in blue;
protomer A of GPLGS-WT is in yellow; inhibitor N3 (complexed
with WT) is in magenta; inhibitor N3 (complexed with GPLGS-WT)
is in red; protomer B* of WT is in green; protomer B of GPLGS-WT
is in cyan. Figure 4. Differences between the complex
structures of WT and GPLGS-WT. (a) Inhibitor N3. (b)
Superposition of the substrate-binding pockets in protomer A of
GPLGS-WT and that in protomer A* of WT. In the WT-N3 complex
structure, the NH[2] group of Ser1 in protomer B* was still
hydrogen-bonded to the carboxylate group of Glu166 and the
carbonyl group of Phe140 in protomer A*, stabilizing the S1
pocket. In the GPLGS-WT-N3 complex structure, however, the two
hydrogen bonds described above were not found. Instead, an
ordered water molecule was observed in the S1 pocket. Protomer
A* of WT is in blue; protomer A of GPLGS-WT is in yellow;
inhibitor N3 (complexed with WT) is in magenta; inhibitor N3
(complexed with GPLGS-WT) is in red; protomer B* of WT is in
green; protomer B of GPLGS-WT is in cyan.
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