5sdt: Difference between revisions
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 3: | Line 3: | ||
<StructureSection load='5sdt' size='340' side='right'caption='[[5sdt]], [[Resolution|resolution]] 1.94Å' scene=''> | <StructureSection load='5sdt' size='340' side='right'caption='[[5sdt]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5sdt]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SDT FirstGlance]. <br> | <table><tr><td colspan='2'>[[5sdt]] is a 8 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=5SDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SDT FirstGlance]. <br> | ||
</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=I9Q:N-(3,4-dihydroxy-9,10-dioxo-9,10-dihydroanthracene-2-sulfonyl)-beta-alanine'>I9Q</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.944Å</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=I9Q:N-(3,4-dihydroxy-9,10-dioxo-9,10-dihydroanthracene-2-sulfonyl)-beta-alanine'>I9Q</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</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=5sdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sdt OCA], [https://pdbe.org/5sdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sdt RCSB], [https://www.ebi.ac.uk/pdbsum/5sdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sdt ProSAT]</span></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=5sdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sdt OCA], [https://pdbe.org/5sdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sdt RCSB], [https://www.ebi.ac.uk/pdbsum/5sdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sdt ProSAT]</span></td></tr> | ||
</table> | </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). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 21: | ||
</div> | </div> | ||
<div class="pdbe-citations 5sdt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5sdt" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Brear P]] | |||
[[Category: Brear | [[Category: Foller A]] | ||
[[Category: Foller | [[Category: Grotli M]] | ||
[[Category: Grotli | [[Category: Hyvonen M]] | ||
[[Category: Hyvonen | [[Category: Lulla A]] | ||
[[Category: Lulla | [[Category: Nain-Perez A]] | ||
[[Category: Nain-Perez | |||