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1ult

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Current revision (23:55, 27 December 2023) (edit) (undo)
 
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<StructureSection load='1ult' size='340' side='right'caption='[[1ult]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='1ult' size='340' side='right'caption='[[1ult]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ult]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ult]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULT 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=CIT:CITRIC+ACID'>CIT</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]] 2.55&#8491;</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/Long-chain-fatty-acid--CoA_ligase Long-chain-fatty-acid--CoA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.3 6.2.1.3] </span></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=CIT:CITRIC+ACID'>CIT</scene></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=1ult FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ult OCA], [https://pdbe.org/1ult PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ult RCSB], [https://www.ebi.ac.uk/pdbsum/1ult PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ult ProSAT], [https://www.topsan.org/Proteins/RSGI/1ult TOPSAN]</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=1ult FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ult OCA], [https://pdbe.org/1ult PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ult RCSB], [https://www.ebi.ac.uk/pdbsum/1ult PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ult ProSAT], [https://www.topsan.org/Proteins/RSGI/1ult TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LCFCS_THET8 LCFCS_THET8]] Catalyzes the esterification of a number of long chain fatty acids with CoA, resulting in the formation of long-chain fatty acyl-CoA. Myristate (C14) is the most efficiently processed fatty acid, followed by palmitate (C16). Also catalyzes the esterification of stearate (C18) and laurate (C12), but at lower efficiency. Does not catalyze the esterification of the unsaturated fatty acids mysteroleic and palmitoleic acids in vitro.<ref>PMID:15145952</ref>
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[https://www.uniprot.org/uniprot/LCFCS_THET8 LCFCS_THET8] Catalyzes the esterification of a number of long chain fatty acids with CoA, resulting in the formation of long-chain fatty acyl-CoA. Myristate (C14) is the most efficiently processed fatty acid, followed by palmitate (C16). Also catalyzes the esterification of stearate (C18) and laurate (C12), but at lower efficiency. Does not catalyze the esterification of the unsaturated fatty acids mysteroleic and palmitoleic acids in vitro.<ref>PMID:15145952</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Long-chain-fatty-acid--CoA ligase]]
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[[Category: Thermus thermophilus]]
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[[Category: Ago, H]]
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[[Category: Ago H]]
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[[Category: Arii, Y]]
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[[Category: Arii Y]]
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[[Category: Hamada, K]]
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[[Category: Hamada K]]
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[[Category: Hisanaga, Y]]
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[[Category: Hisanaga Y]]
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[[Category: Hori, T]]
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[[Category: Hori T]]
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[[Category: Ida, K]]
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[[Category: Ida K]]
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[[Category: Kanda, H]]
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[[Category: Kanda H]]
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[[Category: Kuramitsu, S]]
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[[Category: Kuramitsu S]]
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[[Category: Miyano, M]]
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[[Category: Miyano M]]
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[[Category: Nakatsu, T]]
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[[Category: Nakatsu T]]
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[[Category: Structural genomic]]
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[[Category: Sugahara M]]
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[[Category: Sugahara, M]]
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[[Category: Yamamoto M]]
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[[Category: Yamamoto, M]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S]]
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[[Category: Ligase]]
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[[Category: Rsgi]]
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Current revision

Crystal structure of tt0168 from Thermus thermophilus HB8

PDB ID 1ult

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Proteopedia Page Contributors and Editors (what is this?)

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