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6l06
From Proteopedia
(Difference between revisions)
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<StructureSection load='6l06' size='340' side='right'caption='[[6l06]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='6l06' size='340' side='right'caption='[[6l06]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6l06]] is a 8 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6l06]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L06 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></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=6l06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l06 OCA], [https://pdbe.org/6l06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l06 RCSB], [https://www.ebi.ac.uk/pdbsum/6l06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l06 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PSD_ECOLI PSD_ECOLI] Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Only decarboxylates the lipid-linked form of the serine moiety, and not serine alone or derivatives like phosphoserine or glycerophosphoserine.[HAMAP-Rule:MF_00662]<ref>PMID:4598120</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Ecobd]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Watanabe S]] | |
| - | [[Category: Watanabe | + | [[Category: Watanabe Y]] |
| - | [[Category: Watanabe | + | |
| - | + | ||
| - | + | ||
| - | + | ||
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Current revision
Crystal structure of Escherichia coli phosphatidylserine decarboxylase (apo-form)
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