1pkm

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Current revision (08:08, 14 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pkm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Felis_catus Felis catus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PKM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pkm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Felis_catus Felis catus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PKM FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=1pkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkm OCA], [https://pdbe.org/1pkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pkm RCSB], [https://www.ebi.ac.uk/pdbsum/1pkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkm 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=1pkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkm OCA], [https://pdbe.org/1pkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pkm RCSB], [https://www.ebi.ac.uk/pdbsum/1pkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KPYM_FELCA KPYM_FELCA]] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).
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[https://www.uniprot.org/uniprot/KPYM_FELCA KPYM_FELCA] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1pkm ConSurf].
</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=1pkm ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The three-dimensional structure of cat-muscle pyoruvate kinase has been refined at a resolution of 2.6 A. The details of the structure permit interpretation of the original heavy-atom studies and give insight into the importance of conserved residues in pyruvate kinases and the allosteric behaviour of the enzyme. There are a small number of essential residues which determine the relative orientations of domains and the precise nature of intersubunit contacts. Arginine residues are particularly important.
 
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Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A.,Allen SC, Muirhead H Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):499-504. PMID:15299671<ref>PMID:15299671</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 1pkm" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Felis catus]]
[[Category: Felis catus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pyruvate kinase]]
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[[Category: Allen SC]]
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[[Category: Allen, S C]]
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[[Category: Muirhead H]]
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[[Category: Muirhead, H]]
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[[Category: Kinase]]
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Current revision

THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS

PDB ID 1pkm

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