1zjh

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==Structure of human muscle pyruvate kinase (PKM2)==
==Structure of human muscle pyruvate kinase (PKM2)==
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<StructureSection load='1zjh' size='340' side='right' caption='[[1zjh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='1zjh' size='340' side='right'caption='[[1zjh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1zjh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZJH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1zjh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZJH FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PKM2, PKM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zjh OCA], [https://pdbe.org/1zjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zjh RCSB], [https://www.ebi.ac.uk/pdbsum/1zjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zjh ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zjh OCA], [http://pdbe.org/1zjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zjh RCSB], [http://www.ebi.ac.uk/pdbsum/1zjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zjh ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zj/1zjh_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zj/1zjh_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==
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*[[Pyruvate Kinase|Pyruvate Kinase]]
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*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Pyruvate kinase]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C]]
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[[Category: Arrowsmith C]]
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[[Category: Atanassova, A]]
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[[Category: Atanassova A]]
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[[Category: Bochkarev, A]]
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[[Category: Bochkarev A]]
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[[Category: Choe, J]]
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[[Category: Choe J]]
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[[Category: Edwards, A]]
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[[Category: Edwards A]]
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[[Category: Park, H]]
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[[Category: Park H]]
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[[Category: Structural genomic]]
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[[Category: Sundstrom M]]
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[[Category: Sundstrom, M]]
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[[Category: Allosteric regulation]]
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[[Category: Muscle isozyme]]
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[[Category: Muscpyruvate kinase]]
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[[Category: Sgc]]
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[[Category: Tranferase]]
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[[Category: Transferase]]
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Current revision

Structure of human muscle pyruvate kinase (PKM2)

PDB ID 1zjh

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