1w4h: Difference between revisions

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-==PERIPHERAL-SUBUNIT FROM MESOPHILIC, THERMOPHILIC AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS==
-<StructureSection load='1w4h' size='340' side='right' caption='[[1w4h]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+==Peripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions==
+<StructureSection load='1w4h' size='340' side='right'caption='[[1w4h]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1w4h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W4H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1w4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W4H FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b5s|1b5s]], [[1ebd|1ebd]], [[1lab|1lab]], [[1lac|1lac]], [[1w3d|1w3d]], [[2pdd|2pdd]], [[2pde|2pde]], [[1w4e|1w4e]], [[1w4f|1w4f]], [[1w4g|1w4g]], [[1w4i|1w4i]], [[1w4j|1w4j]], [[1w4k|1w4k]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=1w4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4h OCA], [https://pdbe.org/1w4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w4h RCSB], [https://www.ebi.ac.uk/pdbsum/1w4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w4h ProSAT]</span></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=1w4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4h OCA], [http://pdbe.org/1w4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w4h RCSB], [http://www.ebi.ac.uk/pdbsum/1w4h PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
 == 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/w4/1w4h_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/1w4h_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=1w4h ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 30: @@
 ==See Also==
-*[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]]
+*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
+[[Category: Large Structures]]
-[[Category: Allen, M D]]
+[[Category: Allen MD]]
-[[Category: Ferguson, N]]
+[[Category: Ferguson N]]
-[[Category: Fersht, A R]]
+[[Category: Fersht AR]]
-[[Category: Johnson, C M]]
+[[Category: Johnson CM]]
-[[Category: Schartau, P J]]
+[[Category: Schartau PJ]]
-[[Category: Sharpe, T D]]
+[[Category: Sharpe TD]]
-[[Category: Homologue]]
-[[Category: Peripheral-subunit binding domain]]
-[[Category: Transferase]]
-[[Category: Ultrafast folding]]