1mq0: Difference between revisions

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 ==Crystal Structure of Human Cytidine Deaminase==
-<StructureSection load='1mq0' size='340' side='right' caption='[[1mq0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='1mq0' size='340' side='right'caption='[[1mq0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mq0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MQ0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mq0]] is a 2 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=1MQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQ0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRD:1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE'>BRD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jtk|1jtk]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRD:1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE'>BRD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytidine_deaminase Cytidine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.5 3.5.4.5] </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=1mq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq0 OCA], [https://pdbe.org/1mq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mq0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mq0 ProSAT]</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=1mq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq0 OCA], [http://pdbe.org/1mq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mq0 RCSB], [http://www.ebi.ac.uk/pdbsum/1mq0 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CDD_HUMAN CDD_HUMAN]] This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
+[https://www.uniprot.org/uniprot/CDD_HUMAN CDD_HUMAN] This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mq/1mq0_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mq/1mq0_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=1mq0 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Human cytidine deaminase (CDA) is an enzyme prominent for its role in catalyzing metabolic processing of nucleoside-type anticancer and antiviral agents. It is thus a promising target for the development of small molecule therapeutic adjuvants. We report the first crystal structure of human CDA as a complex with a tight-binding inhibitor, diazepinone riboside 1. The structure reveals that inhibitor 1 is able to establish a canonical pi/pi-interaction with a key active site residue, Phe 137.
-Structure of human cytidine deaminase bound to a potent inhibitor.,Chung SJ, Fromme JC, Verdine GL J Med Chem. 2005 Feb 10;48(3):658-60. PMID:15689149<ref>PMID:15689149</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mq0" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Deaminase|Deaminase]]
+*[[Deaminase 3D structures|Deaminase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Cytidine deaminase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Chung, S J]]
+[[Category: Chung SJ]]
-[[Category: Fromme, J C]]
+[[Category: Fromme JC]]
-[[Category: Verdine, G L]]
+[[Category: Verdine GL]]
-[[Category: Amine hydrolase]]
-[[Category: Anticancer]]
-[[Category: Chemotherapy]]
-[[Category: Diazepinone]]
-[[Category: Drug]]
-[[Category: Edge-to-face interaction]]
-[[Category: Enzyme]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]
-[[Category: Leukemia]]
-[[Category: Phi-phi interaction]]
-[[Category: Protein]]