1zid

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[[Image:1zid.gif|left|200px]]
 
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{{Structure
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==LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR==
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|PDB= 1zid |SIZE=350|CAPTION= <scene name='initialview01'>1zid</scene>, resolution 2.7&Aring;
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<StructureSection load='1zid' size='340' side='right'caption='[[1zid]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZID:ISONICOTINIC-ACETYL-NICOTINAMIDE-ADENINE+DINUCLEOTIDE'>ZID</scene>
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<table><tr><td colspan='2'>[[1zid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZID FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZID:ISONICOTINIC-ACETYL-NICOTINAMIDE-ADENINE+DINUCLEOTIDE'>ZID</scene></td></tr>
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|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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zid OCA], [https://pdbe.org/1zid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zid RCSB], [https://www.ebi.ac.uk/pdbsum/1zid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zid ProSAT], [https://www.topsan.org/Proteins/TBSGC/1zid TOPSAN]</span></td></tr>
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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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</table>
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}}
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== Function ==
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[https://www.uniprot.org/uniprot/INHA_MYCTU INHA_MYCTU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zi/1zid_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zid ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR'''
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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<ref>PMID:9417034</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1zid" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1ZID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZID OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9417034 9417034]
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[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Jacobs Jr WR]]
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[[Category: Jr., W R.Jacobs.]]
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[[Category: Rozwarski DA]]
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[[Category: Rozwarski, D A.]]
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[[Category: Sacchettini JC]]
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[[Category: Sacchettini, J C.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: enoyl-acp reductase]]
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[[Category: inha enzyme]]
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[[Category: isoniazid]]
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[[Category: modified nadh]]
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[[Category: mycolic acid biosynthesis]]
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[[Category: oxidoreductase]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomic]]
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[[Category: tb structural genomics consortium]]
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[[Category: tbsgc]]
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[[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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Current revision

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

PDB ID 1zid

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