Sandbox Reserved 5
From Proteopedia
(Difference between revisions)
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- | == This page is about 4QA4 | + | == This page is about 4QA4. == |
<Structure load='4qa4' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='4qa4' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
- | + | This protein is the Histone deacetylase. | |
+ | *The surface of 4QA4 that interacts histones. Histones are positively charged.Therefore 4QA4 <scene name='54/545854/Charge/1'>has negative charges.</scene> (<font color="blue">positive charges are blue</font>, <font color="red">negative charges are red</font>). | ||
- | + | *<scene name='54/545854/Ligands/1'>The secondary structure of 4QA4. </scene> | |
- | + | (<font color="">positive charges are blue</font>, <font color="red">negative charges are red</font>). | |
- | <scene name='54/545854/Ligands/1'> | + |
Revision as of 06:24, 23 May 2015
This Sandbox is Reserved from May 10, 2015, through July 31, 2015 for use by the class Protein 3D Structure Visualization & Structural Bioinformatics taught by Eric Martz and Keiichi Namba at Osaka University, Japan. This reservation includes Sandbox Reserved 1 through Sandbox Reserved 10. Syllabus. |
To get started:
More help: Getting Started in Proteopedia, Help:Editing, Main Help Page. |
This page is about 4QA4.
|
This protein is the Histone deacetylase.
- The surface of 4QA4 that interacts histones. Histones are positively charged.Therefore 4QA4 (positive charges are blue, negative charges are red).
(positive charges are blue, negative charges are red).