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Figure 3.
Figure 3. The active site of human granzyme A. (a)
Ball-and-stick representation of the bound inhibitor,
D-Phe-Pro-Arg-CMK (carbons, cyan) and residues that frame the
substrate binding pocket depicted in the context of the
molecular surface. The molecular surfaces of the proposed S1'
and S2' subsites are colored in magenta; S1 subsite, orange; S2,
blue; S3, red; S4, green. (b) Ligplot representation showing
direct interactions between GzmA and the bound inhibitor.
D-Phe-Pro-Arg-CMK bonds and carbons are cyan. Bonds between the
irreversible inhibitor and GzmA are magenta. (c) Stereo view of
the refined (2F[o] - F[c]) electron density for the CMK
inhibitor (carbons, yellow) bound to the GzmA active site
(carbons, gray).
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