2qnx

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<StructureSection load='2qnx' size='340' side='right'caption='[[2qnx]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2qnx' size='340' side='right'caption='[[2qnx]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2qnx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QNX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2qnx]] is a 2 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=2QNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QNX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MDX:11-MERCAPTOUNDECANOIC+ACID'>MDX</scene>, <scene name='pdbligand=UDT:O-DECYL+HYDROGEN+THIOCARBONATE'>UDT</scene></td></tr>
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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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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u6s|1u6s]], [[1hzp|1hzp]], [[1u6e|1u6e]], [[1hnj|1hnj]], [[1hnk|1hnk]], [[2qny|2qny]], [[2qnz|2qnz]], [[2qo0|2qo0]], [[2qo1|2qo1]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MDX:11-MERCAPTOUNDECANOIC+ACID'>MDX</scene>, <scene name='pdbligand=UDT:O-DECYL+HYDROGEN+THIOCARBONATE'>UDT</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr>
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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=2qnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qnx OCA], [https://pdbe.org/2qnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qnx RCSB], [https://www.ebi.ac.uk/pdbsum/2qnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qnx ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qnx OCA], [https://pdbe.org/2qnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qnx RCSB], [https://www.ebi.ac.uk/pdbsum/2qnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qnx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FABH_MYCTU FABH_MYCTU]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall.<ref>PMID:10840036</ref>
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[https://www.uniprot.org/uniprot/FABH_MYCTU FABH_MYCTU] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall.<ref>PMID:10840036</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alhamadsheh, M]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Musayev, F]]
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[[Category: Alhamadsheh M]]
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[[Category: Reynolds, K A]]
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[[Category: Musayev F]]
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[[Category: Sachdeva, S]]
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[[Category: Reynolds KA]]
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[[Category: Scarsdale, J N]]
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[[Category: Sachdeva S]]
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[[Category: Wright, H T]]
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[[Category: Scarsdale JN]]
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[[Category: Acyltransferase]]
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[[Category: Wright HT]]
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[[Category: Enzyme inhibitor complex]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Lipid synthesis]]
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[[Category: Mechanism based inhibitor]]
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[[Category: Multifunctional enzyme]]
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[[Category: Myobacterium tuberculosis]]
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[[Category: Structural basis for substrate specificity]]
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[[Category: Transferase]]
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Revision as of 11:36, 30 August 2023

Crystal structure of the complex between the mycobacterium beta-ketoacyl-acyl carrier protein synthase III (FABH) and 11-[(decyloxycarbonyl)dithio]-undecanoic acid

PDB ID 2qnx

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