Ubiquitin conjugating enzyme Ubc6 UBC domain with isopeptide-linked ubiquitin. Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Nov 2024.
Explore 9EYH in 3D Show helices and sheets RCSB PDB PDBe
9EYH contains 21 α-helices and 28 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-19 | 16 | |
| α-helix | 21-22 | 2 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 33-42 | 10 | 1 |
| α-helix | 43-44 | 2 | |
| β-strand | 53-59 | 7 | 1 |
| α-helix | 68-69 | 2 | |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 80 | 1 | 2 |
| α-helix | 104-116 | 13 | |
| β-strand | 124 | 1 | 2 |
| α-helix | 129-145 | 17 | |
| α-helix | 148-153 | 6 | |
| α-helix | 155-168 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-19 | 16 | |
| α-helix | 21-22 | 2 | |
| β-strand | 25-30 | 6 | 3 |
| β-strand | 33-42 | 10 | 3 |
| α-helix | 43-44 | 2 | |
| β-strand | 53-59 | 7 | 3 |
| α-helix | 68-69 | 2 | |
| β-strand | 70-73 | 4 | 3 |
| β-strand | 80 | 1 | 4 |
| β-strand | 89 | 1 | 5 |
| α-helix | 104-116 | 13 | |
| β-strand | 124 | 1 | 4 |
| α-helix | 129-145 | 17 | |
| α-helix | 148-153 | 6 | |
| α-helix | 155-169 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| β-strand | 12-16 | 5 | 6 |
| β-strand | 22 | 1 | 7 |
| α-helix | 23-33 | 11 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 6 |
| β-strand | 48-49 | 2 | 6 |
| β-strand | 55 | 1 | 7 |
| β-strand | 66-71 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 8 |
| β-strand | 12-15 | 4 | 8 |
| β-strand | 22 | 1 | 9 |
| α-helix | 23-33 | 11 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-44 | 3 | 8 |
| β-strand | 49 | 1 | 8 |
| β-strand | 55 | 1 | 9 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-70 | 5 | 8 |
| β-strand | 74 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 6 | A, B | protein | 178 | Saccharomyces cerevisiae | P33296 (AlphaFold model) |
| Ubiquitin-40S ribosomal protein S31 | C, D000 | protein | 76 | Saccharomyces cerevisiae | P05759 (AlphaFold model) |
>9EYH_1 Ubiquitin-conjugating enzyme E2 6 (chains A, B) MATKQAHKRLTKEYKLMVENPPPYILARPNEDNILEWHYIITGPADTPYKGGQYHGTLTF PSDYPYKPPAIRMITPNGRFKPNTRLKLSMSDYHPDTWNPGWSVSTILNGLLSFMTSDEA TTGSITTSDHQKKTLARNSISYNTFQNVRFKLIFPEVVQENVETLEKRKLDELPETGG
>9EYH_2 Ubiquitin-40S ribosomal protein S31 (chains C, D000) MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymes. Swarnkar, A., Leidner, F., Rout, A.K. et al. EMBO J (2024) 43:6705-6739. DOI 10.1038/s44318-024-00301-3 · PubMed
Other PDB entries of the same protein (UniProt P33296 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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