1mq0

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|PDB= 1mq0 |SIZE=350|CAPTION= <scene name='initialview01'>1mq0</scene>, resolution 2.40&Aring;
|PDB= 1mq0 |SIZE=350|CAPTION= <scene name='initialview01'>1mq0</scene>, resolution 2.40&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=BRD:1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE'>BRD</scene>
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|LIGAND= <scene name='pdbligand=BRD:1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE'>BRD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <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>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1jtk|1JTK]]
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1mq0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mq0 RCSB]</span>
}}
}}
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==Overview==
==Overview==
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.
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.
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==Disease==
 
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Known disease associated with this structure: Anemia, congenital dyserythropoietic, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607465 607465]]
 
==About this Structure==
==About this Structure==
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[[Category: Fromme, J C.]]
[[Category: Fromme, J C.]]
[[Category: Verdine, G L.]]
[[Category: Verdine, G L.]]
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[[Category: BRD]]
 
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[[Category: ZN]]
 
[[Category: amine hydrolase]]
[[Category: amine hydrolase]]
[[Category: anticancer]]
[[Category: anticancer]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:31 2008''

Revision as of 19:19, 30 March 2008


PDB ID 1mq0

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: ,
Activity: Cytidine deaminase, with EC number 3.5.4.5
Related: 1JTK


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Human Cytidine Deaminase


Overview

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.

About this Structure

1MQ0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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