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3RIS

Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme

Summary for 3RIS
Entry DOI10.2210/pdb3ris/pdb
Related3IHR
DescriptorUbiquitin carboxyl-terminal hydrolase isozyme L5, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsalpha-beta-alpha fold, cysteine protease, thiol hydrolase, deubiquitinating enzyme, ubiquitin hydrolase, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: Q9Y5K5
Total number of polymer chains4
Total formula weight110849.23
Authors
Das, C.,Permaul, M.,Maiti, T.K. (deposition date: 2011-04-14, release date: 2011-11-09, Last modification date: 2024-02-28)
Primary citationMaiti, T.K.,Permaul, M.,Boudreaux, D.A.,Mahanic, C.,Mauney, S.,Das, C.
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme.
Febs J., 278:4917-4926, 2011
Cited by
PubMed: 21995438
DOI: 10.1111/j.1742-4658.2011.08393.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.398 Å)
Structure validation

222415

数据于2024-07-10公开中

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