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Figure 1.
Fig. 1. The Hm GlcDH structure. (A) The molecular surface
of the dimer of Hm GlcDH to show the electrostatic potential
calculated at 0 M salt concentration, prepared by using the
program GRASP (17, 18). Red corresponds to a surface potential
less than –10 kcal(mol·electron)^–1; blue corresponds
to a potential greater than +10 kcal(mol·electron)^–1.
(B) Stereo view of the location of two of the potassium ions
(lilac spheres). Individual residues are shown in atom colors if
they lie within 3.5 Å of each potassium ion. The remainder
of the polypeptide chain is shown as an alpha carbon trace,
whereas water molecules are depicted as red spheres. The bound
cofactor, NADP, can be seen to lie close to a cation cluster
involving two bound counterions. (C) A close up stereo view,
using standard atom coloring for the protein, to show two fused
pentagonal rings suspended above the hydrophobic chain of
proline 21 and anchored by hydrogen-bonding interactions to the
surrounding water molecules and polar protein atoms.
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