Sandbox Reserved 321: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 8: Line 8:
by Kelly Hrywkiw
by Kelly Hrywkiw


[[Image:Secondary Structure Progression of inhA.pdb|thumb|left|upright=2.0|alt=Secondary Structure Succession of ATP-bound TUTases. Secondary structure residues are ordered from blue to red.|Secondary structure succession of ATP-bound TUTases.]]
[[Image:Secondary Structure of inhA.png|thumb|left|upright=2.0|alt=Secondary Structure Succession of inhA. Secondary structure residues are ordered from blue to red.|Secondary structure succession inhA.]]





Revision as of 21:28, 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

Secondary Structure Succession of inhA. Secondary structure residues are ordered from blue to red.
Secondary structure succession inhA.


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