The structure of the ubiquitin-like modifier FAT10 reveals a novel targeting mechanism for degradation by the 26S proteasome. Determined by X-ray diffraction at 1.93 Å resolution. Released 29 Aug 2018.
Explore 6GF1 in 3D Show helices and sheets RCSB PDB PDBe
6GF1 contains 16 α-helices and 21 β-strands across 3 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 | 5-11 | 7 | 1 |
| α-helix | 15-16 | 2 | |
| β-strand | 17-21 | 5 | 1 |
| β-strand | 26 | 1 | 2 |
| α-helix | 27-38 | 12 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-49 | 5 | 1 |
| β-strand | 52-53 | 2 | 1 |
| α-helix | 54-55 | 2 | |
| β-strand | 59 | 1 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 70-77 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 3 |
| α-helix | 16 | 1 | |
| β-strand | 17-21 | 5 | 3 |
| β-strand | 26 | 1 | 4 |
| α-helix | 27-38 | 12 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-49 | 5 | 3 |
| β-strand | 52-53 | 2 | 3 |
| α-helix | 54-55 | 2 | |
| β-strand | 59 | 1 | 4 |
| α-helix | 61-63 | 3 | |
| α-helix | 65-67 | 3 | |
| β-strand | 70-77 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 5 |
| α-helix | 15-16 | 2 | |
| β-strand | 17-21 | 5 | 5 |
| β-strand | 26 | 1 | 6 |
| α-helix | 27-38 | 12 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-49 | 5 | 5 |
| β-strand | 52-53 | 2 | 5 |
| α-helix | 54-55 | 2 | |
| β-strand | 59 | 1 | 6 |
| α-helix | 60 | 1 | |
| β-strand | 70-77 | 8 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin D | A, B, C | protein | 83 | Homo sapiens | O15205 (AlphaFold model) |
>6GF1_1 Ubiquitin D (chains A, B, C) GASTLTVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSL SSYGIDKEKTIHLTLKVVKPSDE
The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation. Aichem, A., Anders, S., Catone, N. et al. Nat Commun (2018) 9:3321-3321. DOI 10.1038/s41467-018-05776-3 · PubMed
Other PDB entries of the same protein (UniProt O15205 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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