1MQ0

Crystal Structure of Human Cytidine Deaminase

Summary for 1MQ0

• Entry DOI: 10.2210/pdb1mq0/pdb
• Related: 1JTK
• Descriptor: Cytidine Deaminase, ZINC ION, 1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE, ... (4 entities in total)
• Functional Keywords: human, enzyme, cytidine deaminase, amine hydrolase, inhibitor, diazepinone, leukemia, chemotherapy, anticancer, drug, phi-phi interaction, edge-to-face interaction, protein, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 31636.71

Authors

Chung, S.J.,Fromme, J.C.,Verdine, G.L. (deposition date: 2002-09-13, release date: 2003-11-04, Last modification date: 2024-02-14)

Primary citation

Chung, S.J.,Fromme, J.C.,Verdine, G.L.
Structure of human cytidine deaminase bound to a potent inhibitor
J.Med.Chem., 48:658-660, 2005

PubMed Abstract: 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.

PubMed: 15689149
DOI: 10.1021/jm0496279

Experimental method

X-RAY DIFFRACTION (2.4 Å)