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2vjy
From Proteopedia
(Difference between revisions)
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<StructureSection load='2vjy' size='340' side='right'caption='[[2vjy]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2vjy' size='340' side='right'caption='[[2vjy]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2vjy]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2vjy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VJY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALK:(1R)-1-[DIHYDROXY(METHOXY)-LAMBDA^5^-PHOSPHANYL]ETHANOL'>ALK</scene>, <scene name='pdbligand=ALU:METHYL+HYDROGEN+(S)-ACETYLPHOSPHONATE'>ALU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALK:(1R)-1-[DIHYDROXY(METHOXY)-LAMBDA^5^-PHOSPHANYL]ETHANOL'>ALK</scene>, <scene name='pdbligand=ALU:METHYL+HYDROGEN+(S)-ACETYLPHOSPHONATE'>ALU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vk4|2vk4]], [[2g1i|2g1i]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vk4|2vk4]], [[2g1i|2g1i]]</div></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/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </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=2vjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vjy OCA], [https://pdbe.org/2vjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vjy RCSB], [https://www.ebi.ac.uk/pdbsum/2vjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vjy ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 21:00, 20 October 2021
Pyruvate decarboxylase from Kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate
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Categories: Kluyveromyces lactis | Large Structures | Pyruvate decarboxylase | Konig, S | Kutter, S | Weiss, M S | Wille, G | Asymmetric active site | Decarboxylase | Dimer of dimer | Flavoprotein | Lyase | Magnesium | Map | Metal-binding | Methyl acetylphosphonate | Methylacetylphosphonate | Pyruvate | Substrate activation | Thiamine diphosphate | Thiamine pyrophosphate

