8VXJ: Human apolipoprotein A-I

The crystal structure of human apolipoprotein A-I in complex with Fab 55201. Determined by X-ray diffraction at 2.7 Å resolution. Released 27 Aug 2025.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Homo sapiens, Mus musculus
Chains: 6
Atoms: 9,275
Mol. weight: 147.69 kDa
Released: 27 Aug 2025

Explore 8VXJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VXJ contains 41 α-helices and 85 β-strands across 6 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.

Chain A: 5 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	12
β-strand	10-12	3	13
β-strand	17-25	9	12
α-helix	29-31	3
β-strand	34-39	6	13
β-strand	45-51	7	13
β-strand	58-60	3	13
β-strand	68-73	6	12
β-strand	78-84	7	12
α-helix	88-90	3
β-strand	92-99	8	13
β-strand	110-113	4	13
α-helix	114-116	3
β-strand	117-121	5	13
α-helix	124-126	3
β-strand	127	1	14
β-strand	130-134	5	15
β-strand	145-155	11	15
β-strand	156	1	14
β-strand	161-164	4	16
β-strand	173-175	3	15
α-helix	176-178	3
β-strand	179-181	3	15
β-strand	184-194	11	15
β-strand	203-209	7	16
β-strand	214-220	7	16

Chain B: 5 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	17
β-strand	10-13	4	18
β-strand	19-25	7	17
β-strand	33-38	6	18
β-strand	45-49	5	18
β-strand	53-54	2	18
β-strand	62-67	6	17
β-strand	70-75	6	17
α-helix	80-82	3
β-strand	84-90	7	18
β-strand	96-97	2	18
β-strand	101-105	5	18
β-strand	110	1	19
β-strand	113-117	5	20
α-helix	118-120	3
α-helix	121-126	6
β-strand	128-138	11	20
β-strand	139	1	19
β-strand	144-149	6	21
β-strand	152-153	2	21
β-strand	158-162	5	20
α-helix	163-166	4
β-strand	172-181	10	20
α-helix	182-185	4
β-strand	190-197	8	21
β-strand	200-209	10	21

Chains C and D: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	8-18	11
α-helix	20-34	15
α-helix	37-42	6
α-helix	56-63	8
α-helix	69-77	9
α-helix	79-126	48
α-helix	127-129	3
α-helix	130-133	4
α-helix	134-138	5
α-helix	143-182	40

Chain H: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	1
β-strand	10-12	3	2
β-strand	17-25	9	1
α-helix	29-31	3
β-strand	34-39	6	3
β-strand	45-51	7	3
β-strand	58-60	3	3
β-strand	68-73	6	1
β-strand	78-84	7	1
α-helix	88-90	3
β-strand	93-99	7	3
β-strand	110-113	4	3
β-strand	117-118	2	3
β-strand	119-121	3	2
α-helix	124-126	3
β-strand	127	1	4
β-strand	130-134	5	5
β-strand	145-155	11	5
β-strand	156	1	4
β-strand	161-164	4	6
α-helix	165-167	3
β-strand	173-175	3	5
α-helix	176-178	3
β-strand	179-181	3	5
β-strand	184-194	11	5
α-helix	195-197	3
β-strand	203-209	7	6
β-strand	214-220	7	6

Chain L: 5 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	7
β-strand	10-13	4	8
β-strand	19-25	7	7
β-strand	33-38	6	8
β-strand	45-49	5	8
β-strand	53-54	2	8
β-strand	62-67	6	7
β-strand	70-75	6	7
α-helix	80-82	3
β-strand	85-90	6	8
β-strand	96-97	2	8
β-strand	101-105	5	8
β-strand	110	1	9
β-strand	113-117	5	10
α-helix	118-120	3
α-helix	121-126	6
β-strand	128-138	11	10
β-strand	139	1	9
β-strand	144-149	6	11
β-strand	152-153	2	11
β-strand	158-162	5	10
α-helix	163-166	4
β-strand	172-181	10	10
α-helix	182-185	4
β-strand	190-197	8	11
β-strand	200-209	10	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apolipoprotein A-I	C, D	protein	243	Homo sapiens	P02647 (AlphaFold model)
Fab 55201 heavy chain	A, H	protein	224	Mus musculus
Fab 55201 light chain	B, L	protein	212	Mus musculus

Sequence of entity 1 (C, D), FASTA

>8VXJ_1 Apolipoprotein A-I (chains C, D)
DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKL
REQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVE
PLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEA
LKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKL
NTQ

Sequence of entity 2 (A, H), FASTA

>8VXJ_2 Fab 55201 heavy chain (chains A, H)
EVQLQQSGPELVKPGGSLKLSCKASGXXXXXXXMNWVRQSHGKSLEWVAXXXXXXXXXAY
NQKFKGKATLTVDKSSSTAYMELSSLTSEDSAVYYCARXXXXXXXXXXXXXXWGQGTLVT
VSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVL
QSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRD

Sequence of entity 3 (B, L), FASTA

>8VXJ_3 Fab 55201 light chain (chains B, L)
DIQMTQSPSSLSASLGETVTITCXXXXXXXXXXXWYQQKSGQSPKLLVYXXXXXXXGVPA
RFSGSGSGTSYSLTISSLQPEDFGVYYCXXXXXXXXFGGGTKLEIKRADAAPTVSIFPPS
SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL
TKDEYERHNSYTCEATHKTSTSPIVKSFNRNE

Primary citation

The Structure of the Apolipoprotein A-I Monomer Provides Insights Into Its Oligomerisation and Lipid-binding Mechanisms. Tou, H.I., Rosenes, Z., Khandokar, Y. et al. J Mol Biol (2025) 437:169394-169394. DOI 10.1016/j.jmb.2025.169394 · 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…
9PW3 2.73 Å, Cryo-EM structure of renal amyloid fibril from a variant apolipoprotein A-I R173P…
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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