9JSU: Wild-type native PMEL amyloid - polymorph 2

Wild-type native PMEL amyloid - polymorph 2. Determined by electron microscopy at 1.79 Å resolution. Released 9 Oct 2024.

Method
Electron microscopy
Resolution
1.79 Å
Organism
Homo sapiens
Chains
8
Atoms
2,040
Mol. weight
28.89 kDa
Released
9 Oct 2024

Explore 9JSU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9JSU contains 0 α-helices and 24 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.

Chains A, B, C, D, E, F, G and H: 0 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand152-162111
β-strand167-179132
β-strand18213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
M-alphaA, B, C, D, E, F, G, Hprotein33Homo sapiensP40967 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>9JSU_1 M-alpha (chains A, B, C, D, E, F, G, H)
YVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTHT

Primary citation

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:

Browse structure collections

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