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3bjt

From Proteopedia

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[[Image:3bjt.jpg|left|200px]]
 
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{{Structure
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==Pyruvate kinase M2 is a phosphotyrosine binding protein==
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|PDB= 3bjt |SIZE=350|CAPTION= <scene name='initialview01'>3bjt</scene>, resolution 2.50&Aring;
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<StructureSection load='3bjt' size='340' side='right'caption='[[3bjt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Oxl+Binding+Site+For+Residue+A+901'>AC1</scene>, <scene name='pdbsite=AC2:Oxl+Binding+Site+For+Residue+B+902'>AC2</scene>, <scene name='pdbsite=AC3:Oxl+Binding+Site+For+Residue+C+903'>AC3</scene>, <scene name='pdbsite=AC4:Oxl+Binding+Site+For+Residue+D+904'>AC4</scene>, <scene name='pdbsite=AC5:Mg+Binding+Site+For+Residue+A+1'>AC5</scene>, <scene name='pdbsite=AC6:Mg+Binding+Site+For+Residue+B+903'>AC6</scene>, <scene name='pdbsite=AC7:Mg+Binding+Site+For+Residue+C+904'>AC7</scene> and <scene name='pdbsite=AC8:Mg+Binding+Site+For+Residue+D+905'>AC8</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>
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<table><tr><td colspan='2'>[[3bjt]] is a 4 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=3BJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BJT FirstGlance]. <br>
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|ACTIVITY= <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>
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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]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr>
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|DOMAIN=
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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=3bjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bjt OCA], [https://pdbe.org/3bjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bjt RCSB], [https://www.ebi.ac.uk/pdbsum/3bjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bjt ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bjt OCA], [http://www.ebi.ac.uk/pdbsum/3bjt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bjt RCSB]</span>
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== Function ==
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}}
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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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/3bjt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bjt ConSurf].
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<div style="clear:both"></div>
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'''Pyruvate kinase M2 is a phosphotyrosine binding protein'''
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==See Also==
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*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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3BJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BJT OCA].
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Pyruvate kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Wu N]]
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[[Category: Wu, N.]]
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[[Category: acetylation]]
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[[Category: allosteric enzyme]]
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[[Category: alternative splicing]]
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[[Category: glycolysis]]
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[[Category: magnesium]]
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[[Category: metal-binding]]
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[[Category: phosphoprotein]]
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[[Category: polymorphism]]
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[[Category: pyruvate kinase]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:27:03 2008''
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Current revision

Pyruvate kinase M2 is a phosphotyrosine binding protein

PDB ID 3bjt

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