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 DOI | 10.2210/pdb3ris/pdb |
Related | 3IHR |
Descriptor | Ubiquitin carboxyl-terminal hydrolase isozyme L5, SULFATE ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | alpha-beta-alpha fold, cysteine protease, thiol hydrolase, deubiquitinating enzyme, ubiquitin hydrolase, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: Q9Y5K5 |
Total number of polymer chains | 4 |
Total formula weight | 110849.23 |
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 citation | Maiti, 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: 21995438DOI: 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
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