1KRM

Crystal structure of bovine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine riboside

1KRM の概要

• エントリーDOI: 10.2210/pdb1krm/pdb
• 分子名称: adenosine deaminase, ZINC ION, 6-HYDROXY-1,6-DIHYDRO PURINE NUCLEOSIDE, ... (4 entities in total)
• 機能のキーワード: adenosine deaminase, hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Extracellular side : P56658
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40663.36

構造登録者

Kinoshita, T. (登録日: 2002-01-10, 公開日: 2003-01-14, 最終更新日: 2024-03-13)

主引用文献

Kinoshita, T.,Nishio, N.,Nakanishi, I.,Sato, A.,Fujii, T.
Structure of bovine adenosine deaminase complexed with 6-hydroxy-1,6-dihydropurine riboside.
Acta Crystallogr.,Sect.D, 59:299-303, 2003

PubMed Abstract: The crystal structure of adenosine deaminase (ADA) from bovine intestine complexed with a transition-state analogue, 6-hydroxy-1,6-dihydropurine riboside (HDPR), was solved at 2.5 A resolution by the molecular-replacement method using a homology model based on the crystal structure of mouse ADA. The final refinement converged to a crystallographic R factor of 20.7%. The C(alpha) backbone of bovine ADA is mostly superimposable on that of mouse ADA, although mouse ADA itself did not lead to a solution by molecular replacement. HDPR tightly interacts with ADA by means of six hydrogen bonds and is entirely enclosed within the active site. The lid of the envelope consists of two components: one contains two leucine residues, Leu55 and Leu59, and the other contains the backbone atoms Asp182 and Glu183. The C(delta) atoms of the two leucine residues are 3.5 A from the respective N atoms of the backbone. A weak interaction, similar to CH-pi binding, might make it possible to open the lid. Taking account of the movement and observation of this structural feature, the aim is to design novel ADA inhibitors.

PubMed: 12554940
DOI: 10.1107/S090744490202190X

実験手法

X-RAY DIFFRACTION (2.5 Å)