Beta-endorphin amyloid fibril. Determined by solid-state NMR. Released 28 Oct 2020.
Explore 6TUB in 3D Show helices and sheets RCSB PDB PDBe
6TUB contains 0 α-helices and 28 β-strands across 6 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 | 5-9 | 5 | 1 |
| β-strand | 15 | 1 | 2 |
| β-strand | 18 | 1 | 2 |
| β-strand | 22-24 | 3 | 3 |
| β-strand | 27 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 1 |
| β-strand | 15-18 | 4 | 2 |
| β-strand | 22-24 | 3 | 3 |
| β-strand | 27 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-endorphin | A, B, C, D, E, F | protein | 31 | Homo sapiens | P01189 (AlphaFold model) |
>6TUB_1 Beta-endorphin (chains A, B, C, D, E, F) YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE
The three-dimensional structure of human beta-endorphin amyloid fibrils. Seuring, C., Verasdonck, J., Gath, J. et al. Nat Struct Mol Biol (2020) 27:1178-1184. DOI 10.1038/s41594-020-00515-z · PubMed
Other PDB entries of the same protein (UniProt P01189 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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