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1b5s
From Proteopedia
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<StructureSection load='1b5s' size='340' side='right'caption='[[1b5s]], [[Resolution|resolution]] 4.40Å' scene=''> | <StructureSection load='1b5s' size='340' side='right'caption='[[1b5s]], [[Resolution|resolution]] 4.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1b5s]] is a 5 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1b5s]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. The September 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Pyruvate Dehydrogenase Complex'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_9 10.2210/rcsb_pdb/mom_2012_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5S FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5s OCA], [https://pdbe.org/1b5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5s RCSB], [https://www.ebi.ac.uk/pdbsum/1b5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5s ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:39, 19 May 2021
DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS
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Categories: Dihydrolipoyllysine-residue acetyltransferase | Geobacillus stearothermophilus | Large Structures | Pyruvate Dehydrogenase Complex | RCSB PDB Molecule of the Month | Aevarsson, A | Allen, M D | Hol, W G | Izard, T | Kok, A De | Perham, R N | Westphal, A H | Acyltransferase | Dihydrolipoyl acetyltransferase | Dihydrolipoyl transacetylase | E2p | Pyruvate dehydrogenase

