1ead: Difference between revisions

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{{Seed}}
[[Image:1ead.png|left|200px]]


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==ATOMIC STRUCTURE OF THE CUBIC CORE OF THE PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==
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<StructureSection load='1ead' size='340' side='right'caption='[[1ead]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ead]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAO:OXIDIZED+COENZYME+A'>CAO</scene></td></tr>
{{STRUCTURE_1ead|  PDB=1ead  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ead FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ead OCA], [https://pdbe.org/1ead PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ead RCSB], [https://www.ebi.ac.uk/pdbsum/1ead PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ead ProSAT]</span></td></tr>
 
</table>
===ATOMIC STRUCTURE OF THE CUBIC CORE OF THE PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX===
== Function ==
 
[https://www.uniprot.org/uniprot/ODP2_AZOVI ODP2_AZOVI] 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 ==
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==About this Structure==
  </jmolCheckbox>
1EAD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAD OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ead ConSurf].
 
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==Reference==
__TOC__
Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)., Mattevi A, Obmolova G, Kalk KH, Teplyakov A, Hol WG, Biochemistry. 1993 Apr 20;32(15):3887-901. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8471601 8471601]
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Hol WGJ]]
[[Category: Hol, W G.J.]]
[[Category: Mattevi A]]
[[Category: Mattevi, A.]]
[[Category: Dihydrolipoamide acetyltransferase]]
 
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