Solution NMR structure of human RAD18 (198-240) in complex with ubiquitin. Determined by solution NMR. Released 17 May 2017.
Explore 5VF0 in 3D Show helices and sheets RCSB PDB PDBe
5VF0 contains 4 α-helices and 9 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 2-7 | 6 | 1 |
| β-strand | 12-16 | 5 | 1 |
| β-strand | 22 | 1 | 2 |
| α-helix | 23-34 | 12 | |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 48-49 | 2 | 1 |
| β-strand | 55 | 1 | 2 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 201-202 | 2 | 3 |
| β-strand | 211-212 | 2 | 3 |
| α-helix | 216-230 | 15 | |
| α-helix | 232-233 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Polyubiquitin-B | A | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
| E3 ubiquitin-protein ligase RAD18 | B | protein | 46 | Homo sapiens | Q9NS91 (AlphaFold model) |
>5VF0_1 Polyubiquitin-B (chains A) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>5VF0_2 E3 ubiquitin-protein ligase RAD18 (chains B) GHMQVTKVDCPVCGVNIPESHINKHLDSCLSREEKKESLRSSVHKR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of 53BP1 Chromatin Recruitment by RNF168/169 and RAD18. Hu, Q., Botuyan, M.V., Cui, G. et al. Mol Cell (2017) 66:473-487.e9. DOI 10.1016/j.molcel.2017.04.009 · PubMed
Other PDB entries of the same protein (UniProt P0CG47 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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