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Figure 6
(a) Final 2|Fo| – |Fc| map for ΔG6PD–NADP+ in the region of the structural NADP+. Electron density for most of the molecule is in grey and is contoured at 1.25σ. Density for the C-terminal region from 503 is in cyan and is contoured at 1σ. Density for NADP+ is in blue and is contoured at 1.0σ. Residues shown in black are in one subunit of the dimer; those in red are in the other. (b) Potential hydrogen bonds for the structural NADP+ in ΔG6PD–NADP+. Interactions and direct contacts are either with the side chains of surrounding residues or to water molecules (shown in green). The changes in the conformation of NADP+ in ΔG6PD when bound in the structural site or in the coenzyme site (Fig. 4[link]b) are clear.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
Volume 61| Part 5| April 2005| Pages 495-504
doi:10.1107/S0907444905002350
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