3elb
From Proteopedia
(Difference between revisions)
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==Human CTP: Phosphoethanolamine Cytidylyltransferase in complex with CMP== | ==Human CTP: Phosphoethanolamine Cytidylyltransferase in complex with CMP== | ||
- | <StructureSection load='3elb' size='340' side='right' caption='[[3elb]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3elb' size='340' side='right'caption='[[3elb]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3elb]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3elb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ELB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ELB FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCYT2 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCYT2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ethanolamine-phosphate_cytidylyltransferase Ethanolamine-phosphate cytidylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.14 2.7.7.14] </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=3elb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3elb OCA], [https://pdbe.org/3elb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3elb RCSB], [https://www.ebi.ac.uk/pdbsum/3elb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3elb ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/PCY2_HUMAN PCY2_HUMAN]] Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-ethanolamine. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Ethanolamine-phosphate cytidylyltransferase]] | [[Category: Ethanolamine-phosphate cytidylyltransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Andersson, J]] | [[Category: Andersson, J]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] |
Revision as of 11:52, 16 February 2022
Human CTP: Phosphoethanolamine Cytidylyltransferase in complex with CMP
|
Categories: Ethanolamine-phosphate cytidylyltransferase | Human | Large Structures | Andersson, J | Arrowsmith, C H | Berg, S Van Den | Berglund, H | Bountra, C | Collins, R | Dahlgren, L G | Edwards, A M | Flodin, S | Flores, A | Graslund, S | Hammarstrom, M | Johansson, A | Johansson, I | Karlberg, T | Kotenyova, T | Lehtio, L | Moche, M | Nilsson, M E | Nordlund, P | Nyman, T | Persson, C | Structural genomic | Sagemark, J | Schuler, H | Thorsell, A G | Tresaugues, L | Weigelt, J | Welin, M | Wikstrom, M | Wisniewska, M | Cmp | Ctp | Cytidylyltransferase | Kennedy pathway | Nucleotidyltransferase | Phosphoethanolamine | Phospholipid biosynthesis | Sgc | Transferase