3A33
UbcH5b~Ubiquitin Conjugate
Summary for 3A33
| Entry DOI | 10.2210/pdb3a33/pdb |
| Related | 1UBQ 2ESK |
| Descriptor | Ubiquitin-conjugating enzyme E2 D2, Ubiquitin, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | e2 ubiquitin-conjugating enzyme, ubiquitin, ligase, ubl conjugation pathway, isopeptide bond, nucleus |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 25623.30 |
| Authors | Sakata, E.,Satoh, T.,Yamamoto, S.,Yamaguchi, Y.,Yagi-Utsumi, M.,Kurimoto, E.,Wakatsuki, S.,Kato, K. (deposition date: 2009-06-08, release date: 2009-11-24, Last modification date: 2024-11-06) |
| Primary citation | Sakata, E.,Satoh, T.,Yamamoto, S.,Yamaguchi, Y.,Yagi-Utsumi, M.,Kurimoto, E.,Tanaka, K.,Wakatsuki, S.,Kato, K. Crystal Structure of UbcH5b~Ubiquitin Intermediate: Insight into the Formation of the Self-Assembled E2~Ub Conjugates Structure, 18:138-147, 2010 Cited by PubMed Abstract: E2 ubiquitin-conjugating enzymes catalyze the attachment of ubiquitin to lysine residues of target proteins. The UbcH5b E2 enzyme has been shown to play a key role in the initiation of the ubiquitination of substrate proteins upon action of several E3 ligases. Here we have determined the 2.2 A crystal structure of an intermediate of UbcH5b~ubiquitin (Ub) conjugate, which is assembled into an infinite spiral through the backside interaction. This active complex may provide multiple E2 active sites, enabling efficient ubiquitination of substrates. Indeed, biochemical assays support a model in which the self-assembled UbcH5b~Ub can serve as a bridge for the gap between the lysine residue of the substrate and the catalytic cysteine of E2. PubMed: 20152160DOI: 10.1016/j.str.2009.11.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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