1mq0: Difference between revisions

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<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 ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mq0]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/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" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[1jtk|1jtk]]</div></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'>[https://en.wikipedia.org/wiki/Cytidine_deaminase Cytidine deaminase], with EC number [https://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'>[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>
</table>
</table>
== Function ==
== Function ==
[[https://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 ==
== 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=1mq0 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="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==
==See Also==
*[[Deaminase 3D structures|Deaminase 3D structures]]
*[[Deaminase 3D structures|Deaminase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cytidine deaminase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[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]]

Latest revision as of 10:47, 14 February 2024

Crystal Structure of Human Cytidine DeaminaseCrystal Structure of Human Cytidine Deaminase

Structural highlights

1mq0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1mq0, resolution 2.40Å

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OCA
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