2UZG
Zf-UBP domain of VDU1
Summary for 2UZG
| Entry DOI | 10.2210/pdb2uzg/pdb |
| Descriptor | UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 33, ZINC ION (2 entities in total) |
| Functional Keywords | ubl conjugation pathway, de-ubiquitination, alternative splicing, metal-binding, thiol protease, ubl conjugation, zinc, vdu1, zf-ubp, protease, hydrolase, zinc-finger |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm, perinuclear region . Isoform 3: Golgi apparatus : Q8TEY7 |
| Total number of polymer chains | 1 |
| Total formula weight | 11124.56 |
| Authors | Allen, M.D.,Bycroft, M. (deposition date: 2007-04-27, release date: 2007-05-08, Last modification date: 2024-05-15) |
| Primary citation | Allen, M.D.,Bycroft, M. The Solution Structure of the Znf Ubp Domain of Usp33/Vdu1. Protein Sci., 16:2072-, 2007 Cited by PubMed Abstract: USP33/VDU1 is a deubiquitinating enzyme that binds to the von Hippel-Lindau tumor suppressor protein. It also regulates thyroid hormone activation by deubiquitinating type 2 iodothyronine deiodinase. USP33/VDU1 contains a ZF UBP domain, a protein module found in many proteins in the ubiquitin-proteasome system. Several ZF UBP domains have been shown to bind ubiquitin, and a structure of a complex of the ZF UBP domain of isoT/USP5 and ubiquitin is available. In the present work, the solution structure of the ZF UBP domain of USP33/VDU1 has been determined by NMR spectroscopy. The structure differs from that of the USP5 domain, which contains only one of the three Zn ions present in the USP33/VDU1 structure. The USP33/VDU1 ZnF UBP domain does not bind to ubiquitin. PubMed: 17766394DOI: 10.1110/PS.072967807 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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