3h6o
From Proteopedia
(Difference between revisions)
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==Activator-Bound Structure of Human Pyruvate Kinase M2== | ==Activator-Bound Structure of Human Pyruvate Kinase M2== | ||
- | <StructureSection load='3h6o' size='340' side='right' caption='[[3h6o]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3h6o' size='340' side='right'caption='[[3h6o]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3h6o]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3h6o]] is a 4 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=3H6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H6O FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D8G:6-(2-FLUOROBENZYL)-2,4-DIMETHYL-4,6-DIHYDRO-5H-THIENO[2,3 4,5]PYRROLO[2,3-D]PYRIDAZIN-5-ONE'>D8G</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D8G:6-(2-FLUOROBENZYL)-2,4-DIMETHYL-4,6-DIHYDRO-5H-THIENO[2,3 4,5]PYRROLO[2,3-D]PYRIDAZIN-5-ONE'>D8G</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PKM2, PK2, PK3, PKM ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PKM2, PK2, PK3, PKM ([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/Pyruvate_kinase Pyruvate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </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=3h6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h6o OCA], [https://pdbe.org/3h6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h6o RCSB], [https://www.ebi.ac.uk/pdbsum/3h6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h6o ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/KPYM_HUMAN KPYM_HUMAN]] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.<ref>PMID:17308100</ref> <ref>PMID:18191611</ref> <ref>PMID:21620138</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/3h6o_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/3h6o_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
- | *[[Pyruvate | + | *[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Pyruvate kinase]] | [[Category: Pyruvate kinase]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] |
Revision as of 08:04, 16 March 2022
Activator-Bound Structure of Human Pyruvate Kinase M2
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Categories: Human | Large Structures | Pyruvate kinase | Arrowsmith, C H | Auld, D | Bochkarev, A | Bountra, C | Boxer, M | Dimov, S | Edwards, A M | Hong, B | Inglese, J | Jianq, J K | Min, S | Park, H | Structural genomic | Skoumbourdis, A | Southall, N | Tempel, W | Thomas, C | Weigelt, J | Activator | Allosteric enzyme | Glycolysis | Kinase | Magnesium | Metal-binding | Phosphoprotein | Pyruvate | Sgc | Transferase