Sandbox Reserved 5: Difference between revisions

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*<scene name='54/545854/Ligands/1'>The secondary structure of 4QA4. </scene>
*<scene name='54/545854/Ligands/1'>The secondary structure of 4QA4. </scene>
(<font color="pink">alpha helices are pink</font>, <font color="green">beta strands are right green, <font color="yellow"> B3N (4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide) and ZN (Zinc ion) are yellow.</font>).
(<font color="pink">alpha helices are pink</font>, <font color="green">beta strands are right green</font>, <font color="yellow"> 4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide (B3N) and Zinc ion (ZN) are yellow</font>, <font color="blue"> Potassium ion  (K) are blue</font>, </font>).

Revision as of 09:44, 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.
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This page is about 4QA4.This page is about 4QA4.

Insert caption here

Drag the structure with the mouse to rotate

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).


(alpha helices are pink, beta strands are right green, 4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide (B3N) and Zinc ion (ZN) are yellow, Potassium ion (K) are blue, ).

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Eric Martz, Student
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