4FH1
S. cerevisiae Ubc13-N79A
Summary for 4FH1
| Entry DOI | 10.2210/pdb4fh1/pdb |
| Descriptor | Ubiquitin-conjugating enzyme E2 13, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total) |
| Functional Keywords | ubiquitin conjugating enzyme, ligase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 17638.18 |
| Authors | Berndsen, C.E.,Wolberger, C.,Wiener, R. (deposition date: 2012-06-05, release date: 2013-01-09, Last modification date: 2023-09-13) |
| Primary citation | Berndsen, C.E.,Wiener, R.,Yu, I.W.,Ringel, A.E.,Wolberger, C. A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. Nat.Chem.Biol., 9:154-156, 2013 Cited by PubMed Abstract: It is widely accepted that ubiquitin-conjugating enzymes contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and biochemical approaches to study the role of the conserved asparagine to ubiquitin conjugation by Ubc13-Mms2, we conclude that the importance of this residue stems primarily from its structural role in stabilizing an active site loop. PubMed: 23292652DOI: 10.1038/nchembio.1159 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.61 Å) |
Structure validation
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