3IHR
Crystal Structure of Uch37
Summary for 3IHR
| Entry DOI | 10.2210/pdb3ihr/pdb |
| Descriptor | Ubiquitin carboxyl-terminal hydrolase isozyme L5, FORMIC ACID, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | center for eukaryotic structural genomics, uch37, uch-l5, ubiquitin hydrolase, homo sapiens, ubiquitin, proteasome, ino80, smad7, rpn13, psi, protein structure initiative, cesg, structural genomics, hydrolase, protease, thiol protease, ubl conjugation pathway |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : Q9Y5K5 |
| Total number of polymer chains | 1 |
| Total formula weight | 38016.69 |
| Authors | Burgie, E.S.,Bingman, C.A.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2009-07-30, release date: 2009-08-11, Last modification date: 2023-07-26) |
| Primary citation | Burgie, S.E.,Bingman, C.A.,Soni, A.B.,Phillips Jr., G.N. Structural characterization of human Uch37. Proteins, 80:649-654, 2012 Cited by PubMed Abstract: Uch37 is a de-ubiquitylating enzyme that is functionally linked with the 26S proteasome via Rpn13, and is essential for metazoan development. Here, we report the X-ray crystal structure of full-length human Uch37 at 2.95 Å resolution. Uch37's catalytic domain is similar to those of all UCH enzymes characterized to date. The C-terminal extension is elongated, predominantly helical and contains coiled coil interactions. Additionally, we provide an initial characterization of Uch37's oligomeric state and identify a systematic error in previous analyses of Uch37 activity. Taken together, these data provide a strong foundation for further analysis of Uch37's several functions. PubMed: 21953935DOI: 10.1002/prot.23147 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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