Sandbox Reserved 1240

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==<b>Structure</b>==
==<b>Structure</b>==
<StructureSection load='1qki' size='340' side='right' caption='Glucose-6-Phosphate Dehydrogenase at a resolution of 3.0 Å' scene=''>
<StructureSection load='1qki' size='340' side='right' caption='Glucose-6-Phosphate Dehydrogenase at a resolution of 3.0 Å' scene=''>
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Overall, the structure of Glucose-6-Phosphate Dehydrogenase (G6PD) is a tetramer, composed of a dimer of dimers. Glucose-6-Phosphate Dehydrogenase also features a structural nicotinamide adenine, which is only present in eukaryotes and is rare biologically. Glucose-6-Phosphate Dehydrogenase is 515 amino acids long.
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Overall, the structure of Glucose-6-Phosphate Dehydrogenase (<i>G6PD</i>) is a tetramer, composed of a dimer of dimers. Glucose-6-Phosphate Dehydrogenase also features a structural nicotinamide adenine, which is only present in eukaryotes and is rare biologically. Glucose-6-Phosphate Dehydrogenase is 515 amino acids long.
== <b>Function</b> ==
== <b>Function</b> ==
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Glucose-6-Phosphate Dehydrogenase plays a key role in maintaining homeostasis. Not only does it catalyze the rate limiting step of the oxidative pentose phosphate pathway, it maintains the shape of red blood cells by protecting against potential deadly reactive oxygen species. Glucose-6-Phosphate dehydrogenase deficiency is the most common enzyme deficiency in humans, affecting over 400 million people worldwide. G6PD deficiency resulted in 4100 deaths worldwide in 2013
Glucose-6-Phosphate Dehydrogenase plays a key role in maintaining homeostasis. Not only does it catalyze the rate limiting step of the oxidative pentose phosphate pathway, it maintains the shape of red blood cells by protecting against potential deadly reactive oxygen species. Glucose-6-Phosphate dehydrogenase deficiency is the most common enzyme deficiency in humans, affecting over 400 million people worldwide. G6PD deficiency resulted in 4100 deaths worldwide in 2013
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== <b>Structural highlights </b> ==
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== Structural highlights ==
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The two dimers are held together by charge-charge interactions
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 14:49, 20 April 2017

This Sandbox is Reserved from Jan 17 through June 31, 2017 for use in the course Biochemistry II taught by Jason Telford at the Maryville University, St. Louis, USA. This reservation includes Sandbox Reserved 1225 through Sandbox Reserved 1244.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • 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

Structure

Glucose-6-Phosphate Dehydrogenase at a resolution of 3.0 Å

Drag the structure with the mouse to rotate

References

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