2ETL
Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)
Summary for 2ETL
| Entry DOI | 10.2210/pdb2etl/pdb |
| Descriptor | Ubiquitin carboxyl-terminal hydrolase isozyme L1, CHLORIDE ION (3 entities in total) |
| Functional Keywords | deubiquitinating thiol hydrolase, hydrolase, ligase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : P09936 |
| Total number of polymer chains | 2 |
| Total formula weight | 50675.41 |
| Authors | Das, C.,Hoang, Q.Q.,Kreinbring, C.A.,Luchansky, S.J.,Meray, R.K.,Ray, S.S.,Lansbury, P.T.,Ringe, D.,Petsko, G.A. (deposition date: 2005-10-27, release date: 2006-03-28, Last modification date: 2024-04-03) |
| Primary citation | Das, C.,Hoang, Q.Q.,Kreinbring, C.A.,Luchansky, S.J.,Meray, R.K.,Ray, S.S.,Lansbury, P.T.,Ringe, D.,Petsko, G.A. Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1. Proc.Natl.Acad.Sci.USA, 103:4675-4680, 2006 Cited by PubMed: 16537382DOI: 10.1073/pnas.0510403103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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