Sandbox Reserved 321: Difference between revisions

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==Introduction==
==Introduction==


InhA is a enoyl-acyl ACP carrier protein that plays a role in the sysnthesis of Mycolic Acid <ref name="mech of thioamide drug action"/>
InhA is a enoyl-acyl ACP carrier protein that plays a role in the sysnthesis of Mycolic Acid <ref name ="mech of thioamide drug action">
PMID:17227913</ref>.


==Structure==
==Structure==
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==References==
==References==
<Wang F., Langley R., Gulten G., Dover L. G., Besra G. S., Jacobs W. R., and Sacchettini J. C., 2007.  The Journal of Experimental Medicine.  204(1) 73-78="mech of thioamide drug action"/>
 
<references/>

Revision as of 19:07, 30 March 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
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


InhA

by Kelly Hrywkiw


Drag the structure with the mouse to rotate
2h9i, resolution 2.20Å (default scene)
Ligands: EAD
Gene: inhA (Mycobacterium tuberculosis)
Activity: [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9
Related: 1zid
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Introduction

InhA is a enoyl-acyl ACP carrier protein that plays a role in the sysnthesis of Mycolic Acid [1].

Structure

Physiological Function

Role in the Mycolic Acid Pathway

Protein Superfamilly

References

  1. ↑ Wang F, Langley R, Gulten G, Dover LG, Besra GS, Jacobs WR Jr, Sacchettini JC. Mechanism of thioamide drug action against tuberculosis and leprosy. J Exp Med. 2007 Jan 22;204(1):73-8. Epub 2007 Jan 16. PMID:17227913 doi:10.1084/jem.20062100