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1dpd
From Proteopedia
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| - | [[Image:1dpd.png|left|200px]] | ||
| - | + | ==CRYSTALLOGRAPHIC AND ENZYMATIC INVESTIGATIONS ON THE ROLE OF SER558, HIS610 AND ASN614 IN THE CATALYTIC MECHANISM OF AZOTOBACTER VINELANDII DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P)== | |
| + | <StructureSection load='1dpd' size='340' side='right'caption='[[1dpd]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1dpd]] 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=1DPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPD FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=1dpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpd OCA], [https://pdbe.org/1dpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpd RCSB], [https://www.ebi.ac.uk/pdbsum/1dpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpd_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1dpd ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | [[ | + | |
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| - | + | ||
| - | < | + | |
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Hendle | + | [[Category: Hendle J]] |
| - | [[Category: Hol | + | [[Category: Hol WGJ]] |
| - | + | ||
Current revision
CRYSTALLOGRAPHIC AND ENZYMATIC INVESTIGATIONS ON THE ROLE OF SER558, HIS610 AND ASN614 IN THE CATALYTIC MECHANISM OF AZOTOBACTER VINELANDII DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P)
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