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==Crystal structure of human 3-oxoacid CoA transferase 1== | |||
<StructureSection load='3dlx' size='340' side='right'caption='[[3dlx]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3dlx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DLX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3dlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dlx OCA], [https://pdbe.org/3dlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dlx RCSB], [https://www.ebi.ac.uk/pdbsum/3dlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dlx ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/SCOT1_HUMAN SCOT1_HUMAN] Succinyl-CoA:3-ketoacid CoA transferase deficiency. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
== | [https://www.uniprot.org/uniprot/SCOT1_HUMAN SCOT1_HUMAN] Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate. | ||
== Evolutionary Conservation == | |||
[[ | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/3dlx_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=3dlx ConSurf]. | |||
<div style="clear:both"></div> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Bountra | [[Category: Bountra C]] | ||
[[Category: Edwards AM]] | |||
[[Category: Edwards | [[Category: Kavanagh KL]] | ||
[[Category: Kavanagh | [[Category: Maclean EM]] | ||
[[Category: Maclean | [[Category: Murray JW]] | ||
[[Category: Murray | [[Category: Oppermann U]] | ||
[[Category: Oppermann | [[Category: Picaud S]] | ||
[[Category: Picaud | [[Category: Roos AK]] | ||
[[Category: Roos | [[Category: Shafqat N]] | ||
[[Category: Wikstrom M]] | |||
[[Category: Shafqat | [[Category: Yue WW]] | ||
[[Category: Wikstrom | [[Category: Von Delft F]] | ||
[[Category: Yue | |||
[[Category: | |||
Latest revision as of 15:48, 30 August 2023
Crystal structure of human 3-oxoacid CoA transferase 1Crystal structure of human 3-oxoacid CoA transferase 1
Structural highlights
DiseaseSCOT1_HUMAN Succinyl-CoA:3-ketoacid CoA transferase deficiency. The disease is caused by mutations affecting the gene represented in this entry. FunctionSCOT1_HUMAN Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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