Native human Rad6. Determined by X-ray diffraction at 1.5 Å resolution. Released 20 Apr 2011.
Explore 2YB6 in 3D Show helices and sheets RCSB PDB PDBe
2YB6 contains 9 α-helices and 7 β-strands across 1 chain. 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 | 4-18 | 15 | |
| α-helix | 20-21 | 2 | |
| β-strand | 24-29 | 6 | 1 |
| β-strand | 32-41 | 10 | 1 |
| α-helix | 42-43 | 2 | |
| β-strand | 52-58 | 7 | 1 |
| α-helix | 67-68 | 2 | |
| β-strand | 69-72 | 4 | 1 |
| β-strand | 81 | 1 | 2 |
| β-strand | 86 | 1 | 1 |
| β-strand | 87 | 1 | 2 |
| α-helix | 88 | 1 | |
| α-helix | 90-92 | 3 | |
| α-helix | 102-113 | 12 | |
| α-helix | 124-132 | 9 | |
| α-helix | 134-147 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 B | A | protein | 152 | HOMO SAPIENS | P63146 (AlphaFold model) |
>2YB6_1 UBIQUITIN-CONJUGATING ENZYME E2 B (chains A) MSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFS EEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS PANSQAAQLYQENKREYEKRVSAIVEQSWNDS
E3 Ligase Rad18 Promotes Monoubiquitination Rather Than Ubiquitin Chain Formation by E2 Enzyme Rad6. Hibbert, R.G., Huang, A., Boelens, R. et al. Proc Natl Acad Sci U S A (2011) 108:5590. DOI 10.1073/PNAS.1017516108 · PubMed
Other PDB entries of the same protein (UniProt P63146 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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