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2coo
From Proteopedia
(Difference between revisions)
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==Solution structure of the e3_binding domain of dihydrolipoamide branched chaintransacylase== | ==Solution structure of the e3_binding domain of dihydrolipoamide branched chaintransacylase== | ||
| - | <StructureSection load='2coo' size='340' side='right' caption='[[2coo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2coo' size='340' side='right'caption='[[2coo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2coo]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2coo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COO FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DBT, BCATE2 ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DBT, BCATE2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_(2-methylpropanoyl)transferase Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.168 2.3.1.168] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2coo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2coo OCA], [https://pdbe.org/2coo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2coo RCSB], [https://www.ebi.ac.uk/pdbsum/2coo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2coo ProSAT], [https://www.topsan.org/Proteins/RSGI/2coo TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ODB2_HUMAN ODB2_HUMAN]] Defects in DBT are the cause of maple syrup urine disease type 2 (MSUD2) [MIM:[https://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:1847055</ref> <ref>PMID:9621512</ref> |
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ODB2_HUMAN ODB2_HUMAN]] 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). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Hayashi, F]] | [[Category: Hayashi, F]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 11:44, 3 February 2021
Solution structure of the e3_binding domain of dihydrolipoamide branched chaintransacylase
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