1zid

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|GENE=
|GENE=
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0623 FabI], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK07889 PRK07889]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0623 FabI], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK07889 PRK07889]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zid OCA], [http://www.ebi.ac.uk/pdbsum/1zid PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1zid RCSB]</span>
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zid OCA], [http://www.ebi.ac.uk/pdbsum/1zid PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zid RCSB]</span>
}}
}}
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[[Category: tuberculosis]]
[[Category: tuberculosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:18:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:37:01 2008''

Revision as of 22:37, 30 March 2008

Image:1zid.gif


PDB ID 1zid

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands:
Activity: [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9
Domains: FabI, PRK07889
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR


Overview

The preferred antitubercular drug isoniazid specifically targets a long-chain enoyl-acyl carrier protein reductase (InhA), an enzyme essential for mycolic acid biosynthesis in Mycobacterium tuberculosis. Despite the widespread use of this drug for more than 40 years, its precise mode of action has remained obscure. Data from x-ray crystallography and mass spectrometry reveal that the mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of InhA.

About this Structure

1ZID is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis., Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC, Science. 1998 Jan 2;279(5347):98-102. PMID:9417034 [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]

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