2btg: Difference between revisions

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 ==peripheral-subunit binding domains from mesophilic,thermophilic, and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions==
-<StructureSection load='2btg' size='340' side='right' caption='[[2btg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2btg' size='340' side='right'caption='[[2btg]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2btg]] 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=2BTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BTG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2btg]] 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=2BTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BTG FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bal|1bal]], [[1bbl|1bbl]], [[1c4t|1c4t]], [[1e2o|1e2o]], [[1pmr|1pmr]], [[1scz|1scz]], [[2bth|2bth]]</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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=2btg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btg OCA], [https://pdbe.org/2btg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2btg RCSB], [https://www.ebi.ac.uk/pdbsum/2btg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2btg 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=2btg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btg OCA], [http://pdbe.org/2btg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2btg RCSB], [http://www.ebi.ac.uk/pdbsum/2btg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2btg ProSAT]</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]]
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 2btg" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[2-oxoglutarate dehydrogenase 3D structures|2-oxoglutarate dehydrogenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
+[[Category: Large Structures]]
-[[Category: Allen, M D]]
+[[Category: Allen MD]]
-[[Category: Ferguson, N]]
+[[Category: Ferguson N]]
-[[Category: Acyltransferase]]
-[[Category: Lipoyl]]
-[[Category: Transferase]]