2oxy: Difference between revisions

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 ==Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32==
-<StructureSection load='2oxy' size='340' side='right' caption='[[2oxy]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
+<StructureSection load='2oxy' size='340' side='right'caption='[[2oxy]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2oxy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OXY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2oxy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OXY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K17:4,5,6,7-TETRABROMO-BENZIMIDAZOLE'>K17</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]] 1.812&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j91|1j91]], [[1zoh|1zoh]], [[1zog|1zog]], [[1zoe|1zoe]], [[2oxd|2oxd]], [[2oxx|2oxx]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K17:4,5,6,7-TETRABROMO-BENZIMIDAZOLE'>K17</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 MAIZE])</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=2oxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxy OCA], [https://pdbe.org/2oxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oxy RCSB], [https://www.ebi.ac.uk/pdbsum/2oxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oxy ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=2oxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxy OCA], [http://pdbe.org/2oxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oxy RCSB], [http://www.ebi.ac.uk/pdbsum/2oxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oxy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CSK2A_MAIZE CSK2A_MAIZE]] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
+[https://www.uniprot.org/uniprot/CSK2A_MAIZE CSK2A_MAIZE] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
 == 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=2oxy ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote cell survival and enhance the tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K(i) values between 0.15 and 0.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, in an area with a positive electrostatic potential that is able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining the ligand orientation and binding selectivity.
-The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules.,Battistutta R, Mazzorana M, Cendron L, Bortolato A, Sarno S, Kazimierczuk Z, Zanotti G, Moro S, Pinna LA Chembiochem. 2007 Oct 15;8(15):1804-9. PMID:17768728<ref>PMID:17768728</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2oxy" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Casein kinase|Casein kinase]]
+*[[Casein kinase 3D structures|Casein kinase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Maize]]
+[[Category: Large Structures]]
-[[Category: Non-specific serine/threonine protein kinase]]
+[[Category: Zea mays]]
-[[Category: Battistutta, R]]
+[[Category: Battistutta R]]
-[[Category: Cendron, L]]
+[[Category: Cendron L]]
-[[Category: Zanotti, G]]
+[[Category: Zanotti G]]
-[[Category: Inhibitor]]
-[[Category: Protein kinase ck2]]
-[[Category: Tetrabromobenzoimidazole derivative]]
-[[Category: Transferase]]