We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5scd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:00, 22 May 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='5scd' size='340' side='right'caption='[[5scd]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
<StructureSection load='5scd' size='340' side='right'caption='[[5scd]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5scd]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SCD FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5scd]] 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=5SCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SCD 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=I8U:3-hydroxy-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic+acid'>I8U</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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.041&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </span></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=I8U:3-hydroxy-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic+acid'>I8U</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=5scd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5scd OCA], [https://pdbe.org/5scd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5scd RCSB], [https://www.ebi.ac.uk/pdbsum/5scd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5scd 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=5scd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5scd OCA], [https://pdbe.org/5scd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5scd RCSB], [https://www.ebi.ac.uk/pdbsum/5scd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5scd 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 5scd" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5scd" 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: Pyruvate kinase]]
+
[[Category: Brear P]]
-
[[Category: Brear, P]]
+
[[Category: Foller A]]
-
[[Category: Foller, A]]
+
[[Category: Grotli M]]
-
[[Category: Grotli, M]]
+
[[Category: Hyvonen M]]
-
[[Category: Hyvonen, M]]
+
[[Category: Lulla A]]
-
[[Category: Lulla, A]]
+
[[Category: Nain-Perez A]]
-
[[Category: Nain-Perez, A]]
+
-
[[Category: Active site]]
+
-
[[Category: Inhibition]]
+
-
[[Category: Transferase]]
+
-
[[Category: Transferase-transferase inhibitor complex]]
+

Current revision

Structure of liver pyruvate kinase in complex with anthraquinone derivative 58

PDB ID 5scd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5scd"
Personal tools