1mq0: Difference between revisions
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<StructureSection load='1mq0' size='340' side='right' caption='[[1mq0]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1mq0' size='340' side='right' caption='[[1mq0]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mq0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <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> | ||
</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='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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jtk|1jtk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jtk|1jtk]]</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='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'>[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://www.rcsb.org/pdb/explore.do?structureId=1mq0 RCSB], [http://www.ebi.ac.uk/pdbsum/1mq0 PDBsum]</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> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1mq0" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cytidine deaminase]] | [[Category: Cytidine deaminase]] | ||
[[Category: | [[Category: Human]] | ||
[[Category: Chung, S J]] | [[Category: Chung, S J]] | ||
[[Category: Fromme, J C]] | [[Category: Fromme, J C]] | ||
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[[Category: Edge-to-face interaction]] | [[Category: Edge-to-face interaction]] | ||
[[Category: Enzyme]] | [[Category: Enzyme]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
Revision as of 07:14, 11 September 2015
Crystal Structure of Human Cytidine DeaminaseCrystal Structure of Human Cytidine Deaminase
Structural highlights
Function[CDD_HUMAN] This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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