2x13

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Current revision (13:12, 21 August 2024) (edit) (undo)
 
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<table><tr><td colspan='2'>[[2x13]] is a 1 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=2X13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X13 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2x13]] is a 1 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=2X13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X13 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</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]] 1.74&#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=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2x13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x13 OCA], [https://pdbe.org/2x13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x13 RCSB], [https://www.ebi.ac.uk/pdbsum/2x13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x13 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=2x13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x13 OCA], [https://pdbe.org/2x13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x13 RCSB], [https://www.ebi.ac.uk/pdbsum/2x13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x13 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).
[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Enzymes facilitating the transfer of phosphate groups constitute the most extensive protein families across all kingdoms of life. They make up approximately 10% of the proteins found in the human genome. Understanding the mechanisms by which enzymes catalyze these reactions is essential in characterizing the processes they regulate. Metal fluorides can be used as multifunctional tools to study these enzymes. These ionic species bear the same charge as phosphate and the transferring phosphoryl group and, in addition, allow the enzyme to be trapped in catalytically important states with spectroscopically sensitive atoms interacting directly with active site residues. The ionic nature of these phosphate surrogates also allows their removal and replacement with other analogs. Here, we describe the best practices to obtain these complexes, their use in NMR, X-ray crystallography, cryo-EM, and SAXS and describe a new metal fluoride, scandium tetrafluoride, which has significant anomalous signal using soft X-rays.
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Metal fluorides-multi-functional tools for the study of phosphoryl transfer enzymes, a practical guide.,Pellegrini E, Juyoux P, von Velsen J, Baxter NJ, Dannatt HRW, Jin Y, Cliff MJ, Waltho JP, Bowler MW Structure. 2024 Jul 22:S0969-2126(24)00270-3. doi: 10.1016/j.str.2024.07.007. PMID:39106858<ref>PMID:39106858</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2x13" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==

Current revision

The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 3phosphoglycerate

PDB ID 2x13

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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