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1zjh
From Proteopedia
(Difference between revisions)
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<StructureSection load='1zjh' size='340' side='right'caption='[[1zjh]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1zjh' size='340' side='right'caption='[[1zjh]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1zjh]] is a 1 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | + | <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> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Arrowsmith C]] | |
| - | [[Category: Arrowsmith | + | [[Category: Atanassova A]] |
| - | [[Category: Atanassova | + | [[Category: Bochkarev A]] |
| - | [[Category: Bochkarev | + | [[Category: Choe J]] |
| - | [[Category: Choe | + | [[Category: Edwards A]] |
| - | [[Category: Edwards | + | [[Category: Park H]] |
| - | [[Category: Park | + | [[Category: Sundstrom M]] |
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| - | [[Category: Sundstrom | + | |
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Current revision
Structure of human muscle pyruvate kinase (PKM2)
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