1zjh

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Current revision (07:09, 23 August 2023) (edit) (undo)
 
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<StructureSection load='1zjh' size='340' side='right'caption='[[1zjh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<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://proteopedia.org/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://proteopedia.org/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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pyruvate kinase]]
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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: Sundstrom M]]
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[[Category: Structural genomic]]
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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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