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2vgg

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{{STRUCTURE_2vgg| PDB=2vgg | SCENE= }}
 
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===HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT===
 
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{{ABSTRACT_PUBMED_11960989}}
 
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==About this Structure==
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==HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT==
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[[2vgg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1liy 1liy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGG OCA].
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<StructureSection load='2vgg' size='340' side='right'caption='[[2vgg]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
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== Structural highlights ==
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==See Also==
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<table><tr><td colspan='2'>[[2vgg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1liy 1liy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VGG FirstGlance]. <br>
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*[[Pyruvate Kinase|Pyruvate Kinase]]
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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]] 2.74&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
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==Reference==
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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=2vgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgg OCA], [https://pdbe.org/2vgg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vgg RCSB], [https://www.ebi.ac.uk/pdbsum/2vgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vgg ProSAT]</span></td></tr>
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<ref group="xtra">PMID:011960989</ref><references group="xtra"/>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/KPYR_HUMAN KPYR_HUMAN] Defects in PKLR are the cause of pyruvate kinase hyperactivity (PKHYP) [MIM:[https://omim.org/entry/102900 102900]; also known as high red cell ATP syndrome. This autosomal dominant phenotype is characterized by increase of red blood cell ATP.<ref>PMID:9090535</ref> Defects in PKLR are the cause of pyruvate kinase deficiency of red cells (PKRD) [MIM:[https://omim.org/entry/266200 266200]. A frequent cause of hereditary non-spherocytic hemolytic anemia. Clinically, pyruvate kinase-deficient patients suffer from a highly variable degree of chronic hemolysis, ranging from severe neonatal jaundice and fatal anemia at birth, severe transfusion-dependent chronic hemolysis, moderate hemolysis with exacerbation during infection, to a fully compensated hemolysis without apparent anemia.
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== Function ==
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[https://www.uniprot.org/uniprot/KPYR_HUMAN KPYR_HUMAN] Plays a key role in glycolysis (By similarity).
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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/vg/2vgg_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=2vgg ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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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: Abraham, D J.]]
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[[Category: Abraham DJ]]
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[[Category: Bianchi, P.]]
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[[Category: Bianchi P]]
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[[Category: Chiarelli, L R.]]
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[[Category: Chiarelli LR]]
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[[Category: Dolzan, M.]]
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[[Category: Dolzan M]]
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[[Category: Fortin, R.]]
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[[Category: Fortin R]]
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[[Category: Galizzi, A.]]
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[[Category: Galizzi A]]
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[[Category: Mattevi, A.]]
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[[Category: Mattevi A]]
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[[Category: Valentini, G.]]
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[[Category: Valentini G]]
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[[Category: Wang, C.]]
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[[Category: Wang C]]
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[[Category: Zanella, A.]]
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[[Category: Zanella A]]
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[[Category: Disease mutation]]
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[[Category: Glycolysis]]
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[[Category: Kinase]]
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[[Category: Magnesium]]
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[[Category: Metal-binding]]
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[[Category: Phosphorylation]]
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[[Category: Pyruvate]]
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[[Category: Pyruvate kinase in the active r-state]]
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[[Category: Transferase]]
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Current revision

HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT

PDB ID 2vgg

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