7frx: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7frx]] 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=7FRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FRX FirstGlance]. <br>
<table><tr><td colspan='2'>[[7frx]] 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=7FRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FRX 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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=O88:N-{[4-(3,4-dihydroxybenzene-1-sulfonyl)phenyl]methyl}-3,4-dihydroxybenzene-1-sulfonamide'>O88</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]] 1.847&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=O88:N-{[4-(3,4-dihydroxybenzene-1-sulfonyl)phenyl]methyl}-3,4-dihydroxybenzene-1-sulfonamide'>O88</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=7frx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7frx OCA], [https://pdbe.org/7frx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7frx RCSB], [https://www.ebi.ac.uk/pdbsum/7frx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7frx 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=7frx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7frx OCA], [https://pdbe.org/7frx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7frx RCSB], [https://www.ebi.ac.uk/pdbsum/7frx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7frx ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/KPYR_HUMAN KPYR_HUMAN] Plays a key role in glycolysis (By similarity).
[https://www.uniprot.org/uniprot/KPYR_HUMAN KPYR_HUMAN] Plays a key role in glycolysis (By similarity).
==See Also==
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>

Latest revision as of 13:31, 22 May 2024

Structure of liver pyruvate kinase in complex with allosteric modulator 5Structure of liver pyruvate kinase in complex with allosteric modulator 5

Structural highlights

7frx is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.847Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

KPYR_HUMAN Defects in PKLR are the cause of pyruvate kinase hyperactivity (PKHYP) [MIM:102900; also known as high red cell ATP syndrome. This autosomal dominant phenotype is characterized by increase of red blood cell ATP.[1] Defects in PKLR are the cause of pyruvate kinase deficiency of red cells (PKRD) [MIM: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

KPYR_HUMAN Plays a key role in glycolysis (By similarity).

See Also

References

  1. Beutler E, Westwood B, van Zwieten R, Roos D. G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. PMID:9090535 doi:<282::AID-HUMU13>3.0.CO;2-Z 10.1002/(SICI)1098-1004(1997)9:3<282::AID-HUMU13>3.0.CO;2-Z

7frx, resolution 1.85Å

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OCA