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Figure 1.
Structure of hPDE2A (215–900). The asymmetric unit contains
two molecules, A and B, related by a noncrystallographic 2-fold
axis of symmetry, which, in this view, is roughly parallel to
the plane of the paper in the vertical direction. The three
domains are labeled in the figure, as well as the linker helices
LH1 and LH2 that connect them. Molecule B is shown in surface
representation, and molecule A is shown in a ribbons
representation, with the ribbons colored by crystallographic
B-factor, blue being low and red being high. Regions of the
structure with higher B-factors, such as the linker between the
GAF-B domain and the catalytic domain, are expected to be more
flexible. All side chains from molecule A that are within 3.5
Å of molecule B are shown as magenta sticks, The dimer
interface extends over the surface of the entire molecule. The
two catalytic sites in the vicinity of the Zn^2+ and Mg^2+ ions
(shown as gray and green spheres) mutually occlude each other at
the dimer interface. All figures showing the structure were
generated with PyMOL (www.pymol.org).
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