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1scz

From Proteopedia

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Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase

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Retrieved from "http://52.214.119.220/wiki/index.php/1scz"

@@ Line 3: / Line 3: @@
 <StructureSection load='1scz' size='340' side='right'caption='[[1scz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1scz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SCZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1scz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCZ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e2o|1e2o]], [[1c4t|1c4t]]</div></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">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=1scz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scz OCA], [https://pdbe.org/1scz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scz RCSB], [https://www.ebi.ac.uk/pdbsum/1scz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scz ProSAT]</span></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'>[http://proteopedia.org/fgij/fg.htm?mol=1scz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scz OCA], [http://pdbe.org/1scz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1scz RCSB], [http://www.ebi.ac.uk/pdbsum/1scz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1scz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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).
+[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 26: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
+[[Category: Escherichia coli K-12]]
-[[Category: Ecoli]]
 [[Category: Large Structures]]
-[[Category: Arabashi, A]]
+[[Category: Arabashi A]]
-[[Category: Bunzel, B]]
+[[Category: Bunzel B]]
-[[Category: Carson, M]]
+[[Category: Carson M]]
-[[Category: DeLucas, L]]
+[[Category: DeLucas L]]
-[[Category: Gray, R]]
+[[Category: Gray R]]
-[[Category: Huang, W Y]]
+[[Category: Huang W-Y]]
-[[Category: Johnson, D]]
+[[Category: Johnson D]]
-[[Category: Li, S]]
+[[Category: Li S]]
-[[Category: Lin, G]]
+[[Category: Lin G]]
-[[Category: Lu, S]]
+[[Category: Lu S]]
-[[Category: Luan, C H]]
+[[Category: Luan C-H]]
-[[Category: Luo, D]]
+[[Category: Luo D]]
-[[Category: Luo, M]]
+[[Category: Luo M]]
-[[Category: Nagy, L]]
+[[Category: Nagy L]]
-[[Category: Pruett, P]]
+[[Category: Pruett P]]
-[[Category: Qiu, S]]
+[[Category: Qiu S]]
-[[Category: Schormann, N]]
+[[Category: Schormann N]]
-[[Category: Symersky, J]]
+[[Category: Symersky J]]
-[[Category: Tsao, J]]
+[[Category: Tsao J]]
-[[Category: Zhang, Z]]
+[[Category: Zhang Z]]
-[[Category: Cat-like]]
-[[Category: Coa-dependent acyltransferase]]
-[[Category: Mixed beta-sheeet of 6 strand]]
-[[Category: Transferase]]

1scz

From Proteopedia

Current revision

Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase

Structural highlights

Function

Evolutionary Conservation

See Also

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