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; PubMed: 22617491; DOI: 10.1016/j.bmcl.2012.04.124

Experimental method

X-RAY DIFFRACTION (2.35 Å)