Wild-type PMEL CAF amyloid -in vitro polymerized. Determined by electron microscopy at 1.94 Å resolution. Released 9 Oct 2024.
Explore 9JSW in 3D Show helices and sheets RCSB PDB PDBe
9JSW contains 0 α-helices and 16 β-strands across 8 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 | 149-164 | 16 | 1 |
| β-strand | 167-179 | 13 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| M-alpha | A, B, C, D, E, F, G, H | protein | 35 | Homo sapiens | P40967 (AlphaFold model) |
>9JSW_1 M-alpha (chains A, B, C, D, E, F, G, H) SFVYVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTH
Cryo-EM of wild-type and mutant PMEL amyloid cores reveals structural mechanism of pigment dispersion syndrome. Yanagisawa, H., Arai, H., Wang, T. et al. Nat Commun (2025) 16:5411-5411. DOI 10.1038/s41467-025-61233-y · PubMed
Other PDB entries of the same protein (UniProt P40967 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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