4DM9
The Crystal Structure of Ubiquitin Carboxy-terminal hydrolase L1 (UCHL1) bound to a tripeptide fluoromethyl ketone Z-VAE(OMe)-FMK
Summary for 4DM9
Entry DOI | 10.2210/pdb4dm9/pdb |
Related | 2ETL |
Related PRD ID | PRD_001082 |
Descriptor | Ubiquitin carboxyl-terminal hydrolase isozyme L1, Tripeptide fluoromethyl ketone inhibitor Z-VAE(OMe)-FMK (3 entities in total) |
Functional Keywords | ubiquitin hydrolase, ligase, hydrolase, ligase-inhibitor complex, ligase/inhibitor |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P09936 |
Total number of polymer chains | 4 |
Total formula weight | 51533.52 |
Authors | Davies, C.W.,Chaney, J.,Korbel, G.,Ringe, D.,Petsko, G.A.,Ploegh, H.,Das, C. (deposition date: 2012-02-07, release date: 2012-05-23, Last modification date: 2023-09-13) |
Primary citation | Davies, C.W.,Chaney, J.,Korbel, G.,Ringe, D.,Petsko, G.A.,Ploegh, H.,Das, C. The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK). Bioorg.Med.Chem.Lett., 22:3900-3904, 2012 Cited by PubMed: 22617491DOI: 10.1016/j.bmcl.2012.04.124 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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