3g2g
From Proteopedia
(Difference between revisions)
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==S437Y Mutant of human muscle pyruvate kinase, isoform M2== | ==S437Y Mutant of human muscle pyruvate kinase, isoform M2== | ||
- | <StructureSection load='3g2g' size='340' side='right' caption='[[3g2g]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3g2g' size='340' side='right'caption='[[3g2g]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3g2g]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3g2g]] 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=3G2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G2G FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=SO4:SULFATE+ION'>SO4</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=3g2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g2g OCA], [https://pdbe.org/3g2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g2g RCSB], [https://www.ebi.ac.uk/pdbsum/3g2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g2g 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/g2/3g2g_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/3g2g_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: Allali-Hassani, A]] | [[Category: Allali-Hassani, A]] |
Revision as of 20:01, 20 October 2021
S437Y Mutant of human muscle pyruvate kinase, isoform M2
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Categories: Human | Large Structures | Pyruvate kinase | Allali-Hassani, A | Arrowsmith, C H | Bochkarev, A | Bountra, c | Dimov, S | Edwards, A M | Hong, B | MacKenzie, F | Park, H | Structural genomic | Tempel, W | Vedadi, M | Weigelt, J | Acetylation | Allosteric enzyme | Alternative splicing | Glycolysis | Kinase | Magnesium | Metal-binding | Mutation | Phosphoprotein | Polymorphism | Pyruvate | Single nucleotide polymorphism | Snp | Transferase