Crystal structure of the activated aerolysin mutant H132D. Determined by X-ray diffraction at 2.1 Å resolution. Released 9 Feb 2010.
Explore 3G4N in 3D Show helices and sheets RCSB PDB PDBe
3G4N contains 40 α-helices and 55 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| β-strand | 10-12 | 3 | 1 |
| β-strand | 23-25 | 3 | 1 |
| α-helix | 28-33 | 6 | |
| α-helix | 35-39 | 5 | |
| β-strand | 47-49 | 3 | 1 |
| β-strand | 54-57 | 4 | 1 |
| α-helix | 59-61 | 3 | |
| β-strand | 65-67 | 3 | 1 |
| β-strand | 73-77 | 5 | 1 |
| α-helix | 80-82 | 3 | |
| α-helix | 84-90 | 7 | |
| β-strand | 91-93 | 3 | 2 |
| α-helix | 98-106 | 9 | |
| α-helix | 109-113 | 5 | |
| α-helix | 114-122 | 9 | |
| β-strand | 125 | 1 | 3 |
| β-strand | 140-145 | 6 | 2 |
| β-strand | 148-153 | 6 | 2 |
| β-strand | 169-179 | 11 | 2 |
| α-helix | 181-183 | 3 | |
| β-strand | 185-186 | 2 | 2 |
| β-strand | 191-206 | 16 | 2 |
| β-strand | 212 | 1 | 4 |
| β-strand | 215-229 | 15 | 2 |
| α-helix | 234-237 | 4 | |
| β-strand | 239-240 | 2 | 2 |
| β-strand | 245-246 | 2 | 5 |
| α-helix | 247-249 | 3 | |
| β-strand | 258-259 | 2 | 5 |
| α-helix | 260 | 1 | |
| α-helix | 265-267 | 3 | |
| β-strand | 270-281 | 12 | 2 |
| β-strand | 285 | 1 | 4 |
| β-strand | 289-321 | 33 | 2 |
| β-strand | 322 | 1 | 3 |
| α-helix | 323 | 1 | |
| β-strand | 329 | 1 | 6 |
| β-strand | 338-345 | 8 | 2 |
| α-helix | 351-353 | 3 | |
| α-helix | 355-361 | 7 | |
| α-helix | 365-367 | 3 | |
| β-strand | 371 | 1 | 6 |
| α-helix | 373-380 | 8 | |
| α-helix | 382-392 | 11 | |
| β-strand | 396-411 | 16 | 2 |
| β-strand | 415-416 | 2 | 2 |
| β-strand | 420-421 | 2 | 2 |
| β-strand | 442-444 | 3 | 2 |
| α-helix | 449-454 | 6 | |
| β-strand | 458-466 | 9 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 23-25 | 3 | 7 |
| α-helix | 28-33 | 6 | |
| α-helix | 35-39 | 5 | |
| β-strand | 47-50 | 4 | 7 |
| β-strand | 54-57 | 4 | 7 |
| α-helix | 59-61 | 3 | |
| β-strand | 65-67 | 3 | 7 |
| β-strand | 73-77 | 5 | 7 |
| α-helix | 80-82 | 3 | |
| α-helix | 84-86 | 3 | |
| α-helix | 88-90 | 3 | |
| β-strand | 91-93 | 3 | 8 |
| α-helix | 98-106 | 9 | |
| α-helix | 109-113 | 5 | |
| α-helix | 114-123 | 10 | |
| β-strand | 125 | 1 | 9 |
| β-strand | 140-145 | 6 | 8 |
| β-strand | 148-153 | 6 | 8 |
| β-strand | 169-186 | 18 | 8 |
| β-strand | 193-203 | 11 | 8 |
| β-strand | 215-218 | 4 | 10 |
| β-strand | 219-229 | 11 | 8 |
| α-helix | 235-237 | 3 | |
| β-strand | 240 | 1 | 8 |
| β-strand | 245-246 | 2 | 11 |
| α-helix | 247-249 | 3 | |
| β-strand | 258-259 | 2 | 11 |
| β-strand | 270-279 | 10 | 8 |
| β-strand | 292-321 | 30 | 8 |
| β-strand | 322 | 1 | 9 |
| α-helix | 323 | 1 | |
| β-strand | 329 | 1 | 12 |
| β-strand | 338-345 | 8 | 8 |
| α-helix | 351-353 | 3 | |
| α-helix | 355-360 | 6 | |
| α-helix | 365-367 | 3 | |
| β-strand | 371 | 1 | 12 |
| α-helix | 373-380 | 8 | |
| α-helix | 382-392 | 11 | |
| β-strand | 396-416 | 21 | 8 |
| α-helix | 449-454 | 6 | |
| β-strand | 463-466 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Aerolysin | A, B | protein | 470 | Aeromonas hydrophila | P09167 (AlphaFold model) |
>3G4N_1 Aerolysin (chains A, B) AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA HYLGYAWVGGNDSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVT TKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD KRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV PLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ
Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin. Iacovache, I., Degiacomi, M.T., Pernot, L. et al. PLoS Pathog (2011) 7:e1002135-e1002135. DOI 10.1371/journal.ppat.1002135 · PubMed
Other PDB entries of the same protein (UniProt P09167 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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