3LMN

Oligomeric structure of the DUSP domain of human USP15

Summary for 3LMN

• Entry DOI: 10.2210/pdb3lmn/pdb
• Related: 1W6V
• Descriptor: Ubiquitin carboxyl-terminal hydrolase 15, FORMIC ACID, ACETIC ACID, ... (4 entities in total)
• Functional Keywords: 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
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 31163.19

Authors

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. (deposition date: 2010-01-31, release date: 2010-03-23, Last modification date: 2023-09-06)

• Primary citation: 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,

Experimental method

X-RAY DIFFRACTION (2.15 Å)