1umb: Difference between revisions

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<StructureSection load='1umb' size='340' side='right'caption='[[1umb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1umb' size='340' side='right'caption='[[1umb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1umb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMB FirstGlance]. <br>
<table><tr><td colspan='2'>[[1umb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1um9|1um9]], [[1umc|1umc]], [[1umd|1umd]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </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=1umb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umb OCA], [https://pdbe.org/1umb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umb RCSB], [https://www.ebi.ac.uk/pdbsum/1umb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umb ProSAT], [https://www.topsan.org/Proteins/RSGI/1umb TOPSAN]</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=1umb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umb OCA], [https://pdbe.org/1umb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umb RCSB], [https://www.ebi.ac.uk/pdbsum/1umb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umb ProSAT], [https://www.topsan.org/Proteins/RSGI/1umb TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ODBA_THET8 ODBA_THET8]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).[UniProtKB:P37940] [[https://www.uniprot.org/uniprot/ODBB_THET8 ODBB_THET8]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).[UniProtKB:P37941]  
[https://www.uniprot.org/uniprot/ODBA_THET8 ODBA_THET8] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).[UniProtKB:P37940]
== 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: Flavobacterium thermophilum yoshida and oshima 1971]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kamiya, N]]
[[Category: Thermus thermophilus]]
[[Category: Kuramitsu, S]]
[[Category: Kamiya N]]
[[Category: Maoka, N]]
[[Category: Kuramitsu S]]
[[Category: Masui, R]]
[[Category: Maoka N]]
[[Category: Nakagawa, N]]
[[Category: Masui R]]
[[Category: Nakai, T]]
[[Category: Nakagawa N]]
[[Category: Structural genomic]]
[[Category: Nakai T]]
[[Category: Oxidoreductase]]
[[Category: Rsgi]]

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