1s5o: Difference between revisions

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 ==Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase==
-<StructureSection load='1s5o' size='340' side='right' caption='[[1s5o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1s5o' size='340' side='right'caption='[[1s5o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1s5o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S5O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1s5o]] is a 1 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=1S5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S5O FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=152:CARNITINE'>152</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]] 1.8&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=152:CARNITINE'>152</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s5o RCSB], [http://www.ebi.ac.uk/pdbsum/1s5o PDBsum]</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=1s5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5o OCA], [https://pdbe.org/1s5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s5o RCSB], [https://www.ebi.ac.uk/pdbsum/1s5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s5o ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CACP_HUMAN CACP_HUMAN]] Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.
+[https://www.uniprot.org/uniprot/CACP_HUMAN CACP_HUMAN] Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.
 == 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/s5/1s5o_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s5/1s5o_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1s5o ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1s5o" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Carnitine O-acetyltransferase]]
 [[Category: Homo sapiens]]
-[[Category: Agbandje-Mckenna, M]]
+[[Category: Large Structures]]
-[[Category: Govindasamy, L]]
+[[Category: Agbandje-Mckenna M]]
-[[Category: Gu, Y]]
+[[Category: Govindasamy L]]
-[[Category: Jin, S]]
+[[Category: Gu Y]]
-[[Category: Kukar, T]]
+[[Category: Jin S]]
-[[Category: Lian, W]]
+[[Category: Kukar T]]
-[[Category: Mckenna, R]]
+[[Category: Lian W]]
-[[Category: Pedersen, B]]
+[[Category: Mckenna R]]
-[[Category: Wu, D]]
+[[Category: Pedersen B]]
-[[Category: Binary complex]]
+[[Category: Wu D]]
-[[Category: Carnitine acetyltransferase]]
-[[Category: Steady-state enzyme kinetic]]
-[[Category: Substrate binding site]]
-[[Category: Transferase]]