1g0w: Difference between revisions

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 <StructureSection load='1g0w' size='340' side='right'caption='[[1g0w]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1g0w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G0W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1g0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0W FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.3&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatine_kinase Creatine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.2 2.7.3.2] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0w OCA], [http://pdbe.org/1g0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0w RCSB], [http://www.ebi.ac.uk/pdbsum/1g0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0w 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=1g0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0w OCA], [https://pdbe.org/1g0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0w RCSB], [https://www.ebi.ac.uk/pdbsum/1g0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0w ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KCRM_BOVIN KCRM_BOVIN]] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (By similarity).
+[https://www.uniprot.org/uniprot/KCRM_BOVIN KCRM_BOVIN] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (By similarity).
 == Evolutionary Conservation ==
 [[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=1g0w ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Creatine kinase (CK) catalyses the reversible transfer of the phosphate moiety from phosphocreatine (PCr) to ADP, generating creatine and ATP. The crystal structure of a cytosolic brain-type creatine kinase is reported at 2.3 A. The biological dimer sits on a crystallographic twofold axis. The N-terminal residues of both subunits come very close to the crystallographic twofold at the dimer interface. The electron density observed is consistent with two alternative conformations for the N-termini, as previously found for chicken brain-type creatine kinase.
-The three-dimensional structure of cytosolic bovine retinal creatine kinase.,Tisi D, Bax B, Loew A Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):187-93. PMID:11173463<ref>PMID:11173463</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1g0w" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Creatine kinase 3D structures|Creatine kinase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Bos taurus]]
-[[Category: Creatine kinase]]
 [[Category: Large Structures]]
-[[Category: Bax, B]]
+[[Category: Bax B]]
-[[Category: Loew, A]]
+[[Category: Loew A]]
-[[Category: Tisi, D]]
+[[Category: Tisi D]]
-[[Category: Brain-type creatine kinase]]
-[[Category: Guanidino kinase cellular energy metabolism]]
-[[Category: Transferase]]