User:Caitlin Marie Gaich/Sandbox1

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== Structural highlights ==
== Structural highlights ==
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Histone acetyltransferase is an enzyme with two main domains along with a binding site.
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Histone acetyltransferase has an elongated, curved structure with the N and C termini on opposite ends of the structure.
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.
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.

Revision as of 23:27, 27 March 2019

Histone Acetyltransferase HAT1/HAT2 Complex, Saccharomyces cerevisiae

HAT1 4PSW

Drag the structure with the mouse to rotate

References

Li, Y. et. al. Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.(2014). Genes Dev.28:1217-1227. DOI:10.1101/gad.240531.114

  1. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Student Contributors

  • Caitlin Gaich
  • Jordan Finch
  • Morgan Buckley

Proteopedia Page Contributors and Editors (what is this?)

Caitlin Marie Gaich

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