Sandbox Reserved 1563

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<scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.
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<scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.
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<scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.
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<scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.
<scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows.
<scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows.

Revision as of 04:12, 1 December 2019

This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575.
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Inosine-5'-monophosphate dehydrogenase (IMPDH)

Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP

Drag the structure with the mouse to rotate

References

1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.

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