2vgb: Difference between revisions

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-{{Seed}}
-[[Image:2vgb.png|left|200px]]
-<!--
+==HUMAN ERYTHROCYTE PYRUVATE KINASE==
-The line below this paragraph, containing "STRUCTURE_2vgb", creates the "Structure Box" on the page.
+<StructureSection load='2vgb' size='340' side='right'caption='[[2vgb]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2vgb]] 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=1liu 1liu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VGB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.73&#8491;</td></tr>
--->
+<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>
-{{STRUCTURE_2vgb|  PDB=2vgb  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgb OCA], [https://pdbe.org/2vgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vgb RCSB], [https://www.ebi.ac.uk/pdbsum/2vgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vgb ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[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.
+== Function ==
+[https://www.uniprot.org/uniprot/KPYR_HUMAN KPYR_HUMAN] Plays a key role in glycolysis (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/vg/2vgb_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=2vgb ConSurf].
+<div style="clear:both"></div>
-===HUMAN ERYTHROCYTE PYRUVATE KINASE===
+==See Also==
+*[[Pyruvate Kinase|Pyruvate Kinase]]
+*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
-<!--
+== References ==
-The line below this paragraph, {{ABSTRACT_PUBMED_11960989}}, adds the Publication Abstract to the page
+<references/>
-(as it appears on PubMed at http://www.pubmed.gov), where 11960989 is the PubMed ID number.
+__TOC__
--->
+</StructureSection>
-{{ABSTRACT_PUBMED_11960989}}
-==About this Structure==
-VGB is a 4 chains structure of sequences 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=1liu 1liu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGB OCA].
-==Reference==
-<ref group="xtra">PMID:11960989</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Pyruvate kinase]]
+[[Category: Large Structures]]
-[[Category: Abraham, D J.]]
+[[Category: Abraham DJ]]
-[[Category: Bianchi, P.]]
+[[Category: Bianchi P]]
-[[Category: Chiarelli, L.]]
+[[Category: Chiarelli L]]
-[[Category: Dolzan, M.]]
+[[Category: Dolzan M]]
-[[Category: Fortin, R.]]
+[[Category: Fortin R]]
-[[Category: Galizzi, A.]]
+[[Category: Galizzi A]]
-[[Category: Mattevi, A.]]
+[[Category: Mattevi A]]
-[[Category: Valentini, G.]]
+[[Category: Valentini G]]
-[[Category: Wang, C.]]
+[[Category: Wang C]]
-[[Category: Zanella, A.]]
+[[Category: Zanella A]]
-[[Category: Alternative splicing]]
-[[Category: Disease mutation]]
-[[Category: Glycolysis]]
-[[Category: Kinase]]
-[[Category: Magnesium]]
-[[Category: Metal-binding]]
-[[Category: Phosphorylation]]
-[[Category: Polymorphism]]
-[[Category: Pyruvate]]
-[[Category: Pyruvate kinase in the active r-state]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:32:10 2009''