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| + | [[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.]] | ||
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Revision as of 21:21, 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. |
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InhA
by Kelly Hrywkiw
Image:Secondary Structure Progression of inhA.pdb
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| 2h9i, resolution 2.20Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | |||||||||
| 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 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
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
- ↑ 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


