1MQ0

Crystal Structure of Human Cytidine Deaminase

1MQ0 の概要

• エントリーDOI: 10.2210/pdb1mq0/pdb
• 関連するPDBエントリー: 1JTK
• 分子名称: Cytidine Deaminase, ZINC ION, 1-BETA-RIBOFURANOSYL-1,3-DIAZEPINONE, ... (4 entities in total)
• 機能のキーワード: human, enzyme, cytidine deaminase, amine hydrolase, inhibitor, diazepinone, leukemia, chemotherapy, anticancer, drug, phi-phi interaction, edge-to-face interaction, protein, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31636.71

構造登録者

Chung, S.J.,Fromme, J.C.,Verdine, G.L. (登録日: 2002-09-13, 公開日: 2003-11-04, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)