This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1mq0
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1mq0 |SIZE=350|CAPTION= <scene name='initialview01'>1mq0</scene>, resolution 2.40Å | |PDB= 1mq0 |SIZE=350|CAPTION= <scene name='initialview01'>1mq0</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BRD:1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE'>BRD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |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] | + | |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= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jtk|1JTK]] | ||
| + | |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> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==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. | ||
| - | |||
| - | ==Disease== | ||
| - | 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== | ||
| Line 29: | Line 29: | ||
[[Category: Fromme, J C.]] | [[Category: Fromme, J C.]] | ||
[[Category: Verdine, G L.]] | [[Category: Verdine, G L.]] | ||
| - | [[Category: BRD]] | ||
| - | [[Category: ZN]] | ||
[[Category: amine hydrolase]] | [[Category: amine hydrolase]] | ||
[[Category: anticancer]] | [[Category: anticancer]] | ||
| Line 46: | Line 44: | ||
[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
| |||||||
| , 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
Page seeded by OCA on Sun Mar 30 22:19:31 2008
Categories: Cytidine deaminase | Homo sapiens | Single protein | Chung, S J. | Fromme, J C. | Verdine, G L. | Amine hydrolase | Anticancer | Chemotherapy | Diazepinone | Drug | Edge-to-face interaction | Enzyme | Human | Inhibitor | Leukemia | Phi-phi interaction | Protein | Zinc
