3dlx: Difference between revisions

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<StructureSection load='3dlx' size='340' side='right'caption='[[3dlx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3dlx' size='340' side='right'caption='[[3dlx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dlx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OXCT1, OXCT, SCOT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-oxoacid_CoA-transferase 3-oxoacid CoA-transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.5 2.8.3.5] </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=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>
<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>
</table>
== Disease ==
== 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.  
[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 ==
== 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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 3-oxoacid CoA-transferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Delft, F von]]
[[Category: Edwards AM]]
[[Category: Edwards, A M]]
[[Category: Kavanagh KL]]
[[Category: Kavanagh, K L]]
[[Category: Maclean EM]]
[[Category: Maclean, E M]]
[[Category: Murray JW]]
[[Category: Murray, J W]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Picaud S]]
[[Category: Picaud, S]]
[[Category: Roos AK]]
[[Category: Roos, A K]]
[[Category: Shafqat N]]
[[Category: Structural genomic]]
[[Category: Wikstrom M]]
[[Category: Shafqat, N]]
[[Category: Yue WW]]
[[Category: Wikstrom, M]]
[[Category: Von Delft F]]
[[Category: Yue, W W]]
[[Category: Disease mutation]]
[[Category: Mitochondrion]]
[[Category: Oxct1]]
[[Category: Scot]]
[[Category: Sgc]]
[[Category: Succinyl-coa:3-ketoacid-coenzyme a transferase 1]]
[[Category: Transferase]]
[[Category: Transit peptide]]

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

3dlx is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

SCOT1_HUMAN Succinyl-CoA:3-ketoacid CoA transferase deficiency. The disease is caused by mutations affecting the gene represented in this entry.

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

3dlx, resolution 2.20Å

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OCA