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User:Parker Hiday/Sandbox1

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< User:Parker Hiday(Difference between revisions)
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=H. sapiens Lysine Methyltransferase=
=H. sapiens Lysine Methyltransferase=
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load=1O9S size='350' frame='true' side='right' caption='KMT AND 1O9S' scene=’’>
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==Introduction==
==Introduction==
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[[Image:KMT]]
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[[Image:KMT_active_site.png|400 px|left|thumb|Figure 1. The best active site picture you have ever seen!]]
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[https://en.wikipedia.org/wiki/Histone_methyltransferase Wikipedia link of histone methylation]
===Histone Methylation===
===Histone Methylation===
== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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KMT Active Site</scene><scene name='81/811709/Kmt_active_site/1'>Active Site</scene>
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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 ==
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<ref name=”Ransey”>PMID:28504306</ref>
<references/>
<references/>
==Student Contributors==
==Student Contributors==
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Parker Hiday
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Parker Hiday,
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Ashley Crotteau
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Ashley Crotteau,
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Lauren Allman
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and Lauren Allman

Current revision

H. sapiens Lysine Methyltransferase

KMT AND 1O9S

Drag the structure with the mouse to rotate

References

[1]

  1. Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677

Student Contributors

Parker Hiday, Ashley Crotteau, and Lauren Allman

Proteopedia Page Contributors and Editors (what is this?)

Parker Hiday

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