The structure of the ubiquitin-like modifier FAT10 reveals a novel targeting mechanism for degradation by the 26S proteasome. Determined by solution NMR. Released 8 Aug 2018.
Explore 6GF2 in 3D Show helices and sheets RCSB PDB PDBe
6GF2 contains 3 α-helices and 9 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 |
|---|---|---|---|
| β-strand | 8 | 1 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 21-23 | 3 | 2 |
| β-strand | 26 | 1 | 1 |
| β-strand | 31 | 1 | 3 |
| α-helix | 32-42 | 11 | |
| α-helix | 47-49 | 3 | |
| β-strand | 50-53 | 4 | 2 |
| β-strand | 58 | 1 | 2 |
| β-strand | 64 | 1 | 3 |
| α-helix | 65-68 | 4 | |
| β-strand | 74-80 | 7 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin D | A | protein | 85 | Homo sapiens | O15205 (AlphaFold model) |
>6GF2_1 Ubiquitin D (chains A) GAMGDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTLNGKRLE DGKMMADYGIRKGNLLFLASYSIGG
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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