3LMN

Oligomeric structure of the DUSP domain of human USP15

3LMN の概要

• エントリーDOI: 10.2210/pdb3lmn/pdb
• 関連するPDBエントリー: 1W6V
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 15, FORMIC ACID, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: hydrolase, uch, usp, dub, deubiquitylation, deubiquitinating enzyme, ubiquitin, ubiquitin specific protease, ubiquitin carboxyterminal hydrolase, cleavage, usp15, dub15, ubp15, endopeptidase, thiolesterase, dusp, domain-swapping, structural genomics consortium (sgc), acetylation, alternative splicing, phosphoprotein, protease, thiol protease, ubl conjugation pathway
• 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: 31163.19

構造登録者

Walker, J.R.,Asinas, A.,Avvakumov, G.V.,Alenkin, D.,Weigelt, J.,Bountra, C.,Edwards, A.M.,Arrowsmith, C.H.,Bochkarev, A.,Dhe-Paganon, S. (登録日: 2010-01-31, 公開日: 2010-03-23, 最終更新日: 2023-09-06)

• 主引用文献: Walker, J.R.,Asinas, A.,Avvakumov, G.V.,Alenkin, D.,Weigelt, J.,Bountra, C.,Edwards, A.M.,Arrowsmith, C.H.,Bochkarev, A.,Dhe-Paganon, S.; Crystal Structure of the Human Ubiquitin-Specific Protease 15 DUSP Domain; To be Published,

実験手法

X-RAY DIFFRACTION (2.15 Å)