9PVZ: Apolipoprotein A-I

Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient. Determined by electron microscopy at 2.3 Å resolution. Released 18 Mar 2026.

Method
Electron microscopy
Resolution
2.3 Å
Organism
Homo sapiens
Chains
10
Atoms
4,810
Mol. weight
281.21 kDa
Released
18 Mar 2026

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

Secondary structure: helices and β-sheets

9PVZ contains 0 α-helices and 65 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.

Chains A, B, C, D and E: 0 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand16-2381
β-strand2912
β-strand34-3853
β-strand41-4444
β-strand49-5685
β-strand59-6466
β-strand67-7267
Chains F, G, H, I and J: 0 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand16-2388
β-strand2919
β-strand34-441110
β-strand49-56811
β-strand59-64612
β-strand67-72613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apolipoprotein A-IA, B, C, D, E, F, G, H, I, Jprotein243Homo sapiensP02647 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA
>9PVZ_1 Apolipoprotein A-I (chains A, B, C, D, E, F, G, H, I, J)
DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKL
REQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVE
PLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEA
LKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKL
NTQ

Primary citation

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:

Browse structure collections

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