Ubiquitin Variant in Complex with Ubiquitin Interacting Motif. Determined by X-ray diffraction at 2.35 Å resolution. Released 6 Mar 2019.
Explore 6NJG in 3D Show helices and sheets RCSB PDB PDBe
6NJG contains 5 α-helices and 5 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 |
|---|---|---|---|
| α-helix | 1-14 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22 | 1 | 1 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 2 |
| β-strand | 48-49 | 2 | 2 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 1 |
| α-helix | 57-59 | 3 | |
| β-strand | 68-71 | 4 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 27 | B | protein | 24 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40343 (AlphaFold model) |
| Polyubiquitin-B | C | protein | 89 | Homo sapiens | J3QS39 (AlphaFold model) |
>6NJG_1 Vacuolar protein sorting-associated protein 27 (chains B) YPEDEEELIRKAIELSLKESRNSA
>6NJG_2 Polyubiquitin-B (chains C) GGAAQPAMQIFVQTITVMRIALEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGMQLEDG RTLSDYNIKRDSNLYLVSSLRSLRAGAAA
Dimerization of a ubiquitin variant leads to high affinity interactions with a ubiquitin interacting motif. Manczyk, N., Veggiani, G., Gish, G.D. et al. Protein Sci (2019) 28:848-856. DOI 10.1002/pro.3593 · PubMed
Other PDB entries of the same protein (UniProt P40343 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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