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Figure 3.
The two catalytic sites mutually occlude each other at the
dimer interface. (A) The catalytic domain of a single subunit of
the PDE2A (215–900) dimer is shown in ribbons representation,
with the H-loop colored in magenta and the M-loop colored in
blue. The active site, whose location can be inferred from the
position of the Zn^2+ and Mg^2+ ions (shown as gray and green
spheres) is partially occupied by residues from the H-loop.
Residues 840–850 of the M-loop have not been modeled due to
disorder and are indicated by a dotted line. (B) The second
subunit is shown as a semitransparent gray surface, as well as
in ribbons representation, keeping exactly the same orientation
as in panel A. The H-loop is blocked from swinging out of the
active site by the dimer interface.
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