2k7v
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k7v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K7V FirstGlance]. <br> | <table><tr><td colspan='2'>[[2k7v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K7V FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aceF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aceF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k7v RCSB], [http://www.ebi.ac.uk/pdbsum/2k7v PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k7v RCSB], [http://www.ebi.ac.uk/pdbsum/2k7v PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ODP2_ECOLI ODP2_ECOLI]] 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]] | ||
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[[Category: Dihydrolipoyllysine-residue acetyltransferase]] | [[Category: Dihydrolipoyllysine-residue acetyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Jones, D D | + | [[Category: Jones, D D]] |
| - | [[Category: Perham, R N | + | [[Category: Perham, R N]] |
| - | [[Category: Stott, K M | + | [[Category: Stott, K M]] |
| - | [[Category: Yusof, A M | + | [[Category: Yusof, A M]] |
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Glycolysis]] | [[Category: Glycolysis]] | ||
Revision as of 15:20, 25 December 2014
Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form
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