Trapped Toxin. Determined by X-ray diffraction at 2.4 Å resolution. Released 24 Aug 2016.
Explore 5IMY in 3D Show helices and sheets RCSB PDB PDBe
5IMY contains 42 α-helices and 74 β-strands across 4 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 | 48-56 | 9 | |
| α-helix | 64-66 | 3 | |
| β-strand | 67-69 | 3 | 1 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 88-102 | 15 | 1 |
| β-strand | 105-106 | 2 | 2 |
| α-helix | 107 | 1 | |
| α-helix | 112-114 | 3 | |
| β-strand | 120-122 | 3 | 2 |
| α-helix | 125-128 | 4 | |
| β-strand | 134 | 1 | 2 |
| β-strand | 139 | 1 | 3 |
| α-helix | 140-141 | 2 | |
| β-strand | 142-146 | 5 | 2 |
| β-strand | 157-160 | 4 | 2 |
| α-helix | 165-179 | 15 | |
| α-helix | 180-184 | 5 | |
| β-strand | 190 | 1 | 4 |
| α-helix | 191 | 1 | |
| β-strand | 192-199 | 8 | 2 |
| α-helix | 203-210 | 8 | |
| α-helix | 214-217 | 4 | |
| α-helix | 219-221 | 3 | |
| α-helix | 225-229 | 5 | |
| β-strand | 234-249 | 16 | 2 |
| α-helix | 250-251 | 2 | |
| β-strand | 259 | 1 | 3 |
| α-helix | 266-269 | 4 | |
| β-strand | 274 | 1 | 5 |
| β-strand | 277 | 1 | 5 |
| β-strand | 279-297 | 19 | 2 |
| α-helix | 304-312 | 9 | |
| α-helix | 324-327 | 4 | |
| β-strand | 331-337 | 7 | 2 |
| α-helix | 352-361 | 10 | |
| β-strand | 364 | 1 | 4 |
| β-strand | 373-380 | 8 | 2 |
| α-helix | 385 | 1 | |
| β-strand | 386 | 1 | 2 |
| α-helix | 387 | 1 | |
| β-strand | 389-403 | 15 | 1 |
| β-strand | 406-415 | 10 | 6 |
| β-strand | 418 | 1 | 7 |
| β-strand | 421-429 | 9 | 8 |
| β-strand | 435-441 | 7 | 8 |
| β-strand | 449 | 1 | 7 |
| β-strand | 452-459 | 8 | 6 |
| β-strand | 464-469 | 6 | 8 |
| β-strand | 472 | 1 | 7 |
| β-strand | 477 | 1 | 9 |
| β-strand | 479 | 1 | 9 |
| α-helix | 480-481 | 2 | |
| β-strand | 482 | 1 | 7 |
| α-helix | 483 | 1 | |
| β-strand | 486-490 | 5 | 8 |
| β-strand | 495-503 | 9 | 6 |
| β-strand | 506-511 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 67-69 | 3 | 1 |
| β-strand | 77-81 | 5 | 1 |
| β-strand | 87 | 1 | 13 |
| β-strand | 90-102 | 13 | 1 |
| β-strand | 105-106 | 2 | 14 |
| α-helix | 109-112 | 4 | |
| β-strand | 120-122 | 3 | 14 |
| α-helix | 125-128 | 4 | |
| α-helix | 132-133 | 2 | |
| β-strand | 134 | 1 | 14 |
| β-strand | 139 | 1 | 15 |
| α-helix | 140-141 | 2 | |
| β-strand | 142-146 | 5 | 14 |
| β-strand | 157-160 | 4 | 14 |
| α-helix | 165-182 | 18 | |
| β-strand | 192-199 | 8 | 14 |
| α-helix | 203-210 | 8 | |
| α-helix | 214-217 | 4 | |
| α-helix | 226-229 | 4 | |
| β-strand | 234-249 | 16 | 14 |
| β-strand | 257 | 1 | 15 |
| β-strand | 259 | 1 | 15 |
| α-helix | 265-268 | 4 | |
| β-strand | 279-297 | 19 | 14 |
| α-helix | 304-312 | 9 | |
| α-helix | 322-327 | 6 | |
| β-strand | 331-336 | 6 | 14 |
| β-strand | 344 | 1 | 14 |
| α-helix | 352-362 | 11 | |
| β-strand | 373-380 | 8 | 14 |
| α-helix | 385 | 1 | |
| β-strand | 386 | 1 | 14 |
| α-helix | 387 | 1 | |
| β-strand | 389-401 | 13 | 1 |
| β-strand | 404 | 1 | 13 |
| β-strand | 406-412 | 7 | 16 |
| β-strand | 417-429 | 13 | 12 |
| β-strand | 435-441 | 7 | 12 |
| β-strand | 453-459 | 7 | 16 |
| β-strand | 464-473 | 10 | 12 |
| β-strand | 483-490 | 8 | 12 |
| β-strand | 495-502 | 8 | 16 |
| β-strand | 507-514 | 8 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 10 |
| β-strand | 16-18 | 3 | 10 |
| β-strand | 25-31 | 7 | 8 |
| β-strand | 34-40 | 7 | 8 |
| α-helix | 42-44 | 3 | |
| α-helix | 47-54 | 8 | |
| β-strand | 60-64 | 5 | 8 |
| α-helix | 72-74 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vaginolysin | A, B | protein | 490 | Gardnerella vaginalis | B2YGA4 (AlphaFold model) |
| CD59 glycoprotein | C, D | protein | 78 | Homo sapiens | P13987 (AlphaFold model) |
>5IMY_1 Vaginolysin (chains A, B) SNAHMAPSAKDSEPATSCAAKKDSLNNYLWDLQYDKTNILARHGETIENKFSSDSFNKNG EFVVVEHQKKNITNTTSNLSVTSANDDRVYPGALFRADKNLMDNMPSLISANRAPITLSV DLPGFHGGESAVTVQRPTKSSVTSAVNGLVSKWNAQYGASHHVAARMQYDSASAQSMNQL KAKFGADFAKIGVPLKIDFDAVHKGEKQTQIVNFKQTYYTVSVDAPDSPADFFAPCTTPD SLKNRGVDNKRPPVYVSNVAYGRSMYVKFDTTSKSTDFQAAVEAAIKGVEIKPNTEFHRI LQNTSVCAVILGGSANGAAKVCTGNIDTLKALIQEGANLSTSSPAVPIAYTTSFVKDNEV ATLQSNSDYIETKVSSYRNGYLTLDHRGAYVARYYIYWDEYGTEIDGTPYVRSRAWEGNG KYRTAHFNTTIQFKGNVRNLRIKLVEKTGLVWEPWRTVYDRSDLPLVRQRTISNWGTTLW PRVAETVKND
>5IMY_2 CD59 glycoprotein (chains C, D) MLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENEL TYYCCKKDLCNFNEQLEN
Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins. Lawrence, S.L., Gorman, M.A., Feil, S.C. et al. Structure (2016) 24:1488-1498. DOI 10.1016/j.str.2016.06.017 · PubMed
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