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{{STRUCTURE_2g50|  PDB=2g50  |  SCENE=  }}
===The location of the allosteric amino acid binding site of muscle pyruvate kinase.===
{{ABSTRACT_PUBMED_16634623}}


==About this Structure==
==The location of the allosteric amino acid binding site of muscle pyruvate kinase.==
[[2g50]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G50 OCA].  
<StructureSection load='2g50' size='340' side='right'caption='[[2g50]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2g50]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G50 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ETE:2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>ETE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></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=2g50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g50 OCA], [https://pdbe.org/2g50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g50 RCSB], [https://www.ebi.ac.uk/pdbsum/2g50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g50 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KPYM_RABIT KPYM_RABIT] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/2g50_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2g50 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Pyruvate Kinase|Pyruvate Kinase]]
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:016634623</ref><references group="xtra"/>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Pyruvate kinase]]
[[Category: Fenton AW]]
[[Category: Fenton, A W.]]
[[Category: Holyoak T]]
[[Category: Holyoak, T.]]
[[Category: Williams R]]
[[Category: Williams, R.]]
[[Category: Allostery]]
[[Category: Glycolysis]]
[[Category: Kinase]]
[[Category: Phosphoryl transfer]]
[[Category: Pyruvate kinase]]
[[Category: Transferase]]