9IGN: Aerolysin

Aerolysin E254A/E258A in styrene-maleic acid lipid particles. Determined by electron microscopy at 2.3 Å resolution. Released 26 Nov 2025.

Method: Electron microscopy
Resolution: 2.3 Å
Organism: Aeromonas hydrophila
Chains: 14
Atoms: 39,116
Mol. weight: 658.97 kDa
Released: 26 Nov 2025

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

Secondary structure: helices and β-sheets

9IGN contains 231 α-helices and 315 β-strands across 14 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 and G: 16 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	10-12	3	1
β-strand	15	1	2
β-strand	18	1	2
β-strand	23-25	3	1
α-helix	26-27	2
α-helix	28-33	6
α-helix	35-40	6
β-strand	47-49	3	3
β-strand	54-57	4	3
α-helix	59-61	3
β-strand	65-67	3	3
β-strand	73-77	5	1
α-helix	80-82	3
α-helix	84-86	3
α-helix	88-90	3
β-strand	91-93	3	4
α-helix	94	1
α-helix	98-106	9
α-helix	114-123	10
β-strand	125	1	5
β-strand	140-145	6	4
β-strand	148-153	6	4
β-strand	169-179	11	4
α-helix	181-183	3
β-strand	185-186	2	6
β-strand	306-307	2	6
β-strand	308-321	14	4
β-strand	322	1	5
β-strand	329	1	7
β-strand	338-345	8	4
α-helix	355-360	6
α-helix	365-367	3
β-strand	371	1	7
α-helix	373-380	8
α-helix	382-392	11
β-strand	396-400	5	4

Chains H, I, J, K, L, M and N: 17 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	10-12	3	50
β-strand	23-25	3	50
α-helix	26-27	2
α-helix	28-33	6
α-helix	35-39	5
β-strand	47-49	3	50
β-strand	54-57	4	50
α-helix	59-61	3
β-strand	65-67	3	50
β-strand	73-77	5	50
α-helix	80-82	3
α-helix	84-86	3
α-helix	88-90	3
β-strand	91-96	6	51
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-123	10
β-strand	125	1	52
β-strand	140-145	6	51
β-strand	148-153	6	51
β-strand	169-179	11	51
α-helix	181-183	3
β-strand	185-186	2	51
β-strand	190-206	17	51
β-strand	212	1	53
β-strand	215-245	31	54
β-strand	253-281	29	54
β-strand	285	1	53
β-strand	289-321	33	51
β-strand	322	1	52
β-strand	329	1	55
β-strand	338-345	8	51
α-helix	351-353	3
α-helix	355-359	5
α-helix	365-367	3
β-strand	371	1	55
α-helix	373-380	8
α-helix	382-392	11
β-strand	396-416	21	51
β-strand	420-421	2	51

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Aerolysin	A, B, C, D, E, F, G, H, I, J, K, L, M, N	protein	424	Aeromonas hydrophila	P09167 (AlphaFold model)

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

>9IGN_1 Aerolysin (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG
YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA
HYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD
PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVT
TKNKFKWPLVGETALSIAIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA
DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD
KRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV
PLAA

Primary citation

Lumen charge governs gated ion transport in beta-barrel nanopores. Mayer, S.F., Mitsioni, M.F., Robin, P. et al. Nat Nanotechnol (2026) 21:116-124. DOI 10.1038/s41565-025-02052-6 · PubMed

Other PDB entries of the same protein (UniProt P09167 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3G4N 2.1 Å, Crystal structure of the activated aerolysin mutant H132D
9FNQ 2.1 Å, Aerolysin double mutant K238A/K244A in styrene-maleic acid lipid particles
3C0N 2.2 Å, Crystal structure of the proaerolysin mutant Y221G at 2.2 A
9FM6 2.2 Å, Aerolysin Wildtype in styrene-maleic acid lipid particles
9FML 2.2 Å, Aerolysin heptamer in membrane inserted form reconstituted in amphipoles.
9FMX 2.2 Å, Aerolysin Y221G - prepore
9FNP 2.2 Å, Aerolysin mutant K238A in styrene-maleic acid lipid particles
3G4O 2.3 Å, Crystal structure of the activated aerolysin mutant H132N
9GXJ 2.3 Å, Aerolysin E254A/E258A in styrene-maleic acid lipid particles
1Z52 2.38 Å, Proaerolysin Mutant W373L
3C0O 2.5 Å, Crystal structure of the proaerolysin mutant Y221G complexed with mannose-6-phosphate
1PRE 2.8 Å, Proaerolysin

Browse structure collections

About this viewer

MolViewer shows 9IGN directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.