Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I L90P amyloidosis patient. Determined by electron microscopy at 2.15 Å resolution. Released 18 Mar 2026.
Explore 9PVY in 3D Show helices and sheets RCSB PDB PDBe
9PVY contains 0 α-helices and 60 β-strands across 10 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 | 16-23 | 8 | 1 |
| β-strand | 27-29 | 3 | 2 |
| β-strand | 34-44 | 11 | 3 |
| β-strand | 49-56 | 8 | 4 |
| β-strand | 59-64 | 6 | 5 |
| β-strand | 67-72 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 16-23 | 8 | 7 |
| β-strand | 29 | 1 | 8 |
| β-strand | 34-44 | 11 | 9 |
| β-strand | 49-56 | 8 | 10 |
| β-strand | 59-64 | 6 | 11 |
| β-strand | 67-72 | 6 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apolipoprotein A-I | A, B, C, D, E, F, G, H, I, J | protein | 243 | Homo sapiens | P02647 (AlphaFold model) |
>9PVY_1 Apolipoprotein A-I (chains A, B, C, D, E, F, G, H, I, J) DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKL REQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVE PLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEA LKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKL NTQ
Cryo-EM reveals structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations. Nguyen, B.A., Fernandez-Ramirez, M.D.C., Bassett, P. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-72150-z · PubMed
Other PDB entries of the same protein (UniProt P02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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