9PW3: Apolipoprotein A-I

Cryo-EM structure of renal amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient. Determined by electron microscopy at 2.73 Å resolution. Released 18 Mar 2026.

Method: Electron microscopy
Resolution: 2.73 Å
Organism: Homo sapiens
Chains: 10
Atoms: 4,650
Mol. weight: 281.21 kDa
Released: 18 Mar 2026

Explore 9PW3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PW3 contains 0 α-helices and 70 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

Element	Residues	Length	Sheet
β-strand	16-21	6	1
β-strand	29	1	2
β-strand	34-39	6	3
β-strand	42-45	4	4
β-strand	49-56	8	5
β-strand	59-63	5	6
β-strand	67-71	5	7

Chains F and H: 0 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	16-23	8	8
β-strand	29	1	9
β-strand	34-38	5	10
β-strand	41-45	5	11
β-strand	49-56	8	12
β-strand	59-64	6	13
β-strand	67-71	5	14

Chains G, I and J: 0 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	8
β-strand	29	1	9
β-strand	34-38	5	10
β-strand	41-45	5	11
β-strand	49-56	8	12
β-strand	59-64	6	13
β-strand	67-71	5	14

Molecules and chains

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)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA

>9PW3_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:

7KJR 2.08 Å, Cryo-EM structure of SARS-CoV-2 ORF3a
9PVY 2.15 Å, Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I L90P…
3R2P 2.2 Å, 2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals…
9PVZ 2.3 Å, Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I R173P…
8VXJ 2.7 Å, The crystal structure of human apolipoprotein A-I in complex with Fab 55201
8EQS 3.1 Å, Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc
1AV1 4.0 Å, Crystal structure of human apolipoprotein a-I
4V6M 7.1 Å, Structure of the ribosome-SecYE complex in the membrane environment
9MXZ 9.8 Å, Lecithin:Cholesterol Acyltransferase Bound to Apolipoprotein A-I dimer in HDL
1GW3 The helix-hinge-helix structural motif in human apolipoprotein a-I determined by NMR…
1GW4 The helix-hinge-helix structural motif in human apolipoprotein a-I determined by NMR…
1ODP Peptide of human apoa-I residues 166-185. NMR, 5 structures at PH 6.6, 37 degrees…

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