5EGG
Crystal structure of human ubiquitin-conjugating enzyme UBCH5C
Summary for 5EGG
Entry DOI | 10.2210/pdb5egg/pdb |
Descriptor | Ubiquitin-conjugating enzyme E2 D3 (2 entities in total) |
Functional Keywords | biquitin-conjugating enzyme, transferase |
Biological source | Homo sapiens (Human) |
Cellular location | Cell membrane ; Peripheral membrane protein : P61077 |
Total number of polymer chains | 1 |
Total formula weight | 17780.32 |
Authors | |
Primary citation | Wu, F.,Zhu, J.,Li, H.,Zhu, L. Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c Acta Pharm Sin B, 7:390-394, 2017 Cited by PubMed Abstract: UbcH5c belongs to the ubiquitin-conjugating enzyme family and plays an important role in catalyzing ubiquitination during TNF---triggered NF-B activation. Therefore, UbcH5c is a potent therapeutic target for the treatment of inflammatory and autoimmune diseases induced by aberrant activation of NF-B. In this study, we established a stable expression system for recombinant UbcH5c and solved the crystal structure of UbcH5c belonging to space group P222 with one molecule in the asymmetric unit. This study provides the basis for further study of UbcH5c including the design of UbcH5c inhibitors. PubMed: 28540177DOI: 10.1016/j.apsb.2016.12.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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