Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase

Kotaka, M.; Gover, S.; Vandeputte-Rutten, L.; Au, S.W.N.; Lam, V.M.S.; Adams, M.J.

doi:10.1107/S0907444905002350

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 5
Stereoview of the proximity of coenzyme and substrate. The coenzymes seen in ΔG6PD–NADP⁺ and G6P, superimposed from the ΔG6PD–G6P structure, are drawn with C atoms coloured cream. Residues important in binding or catalysis are drawn in cyan; other portions of the chain are drawn in black. Also superimposed (in green) are residues 170–172 (EKP) from subunit A of G6PD_Canton, in which Pro172 is trans; the effect on Lys171 of the change to cis Pro172 in ΔG6PD–NADP⁺ and ΔG6PD–G6P is evident.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 61| Part 5| April 2005| Pages 495-504

doi:10.1107/S0907444905002350

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