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Sandbox Reserved 1563

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=='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==
=='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==
<StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''>
<StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== '''Function(s) and Biological Relevance''' ==
== '''Function(s) and Biological Relevance''' ==

Revision as of 01:33, 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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

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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