Trapped Toxin. Determined by X-ray diffraction at 2.89 Å resolution. Released 24 Aug 2016.
Explore 5IMW in 3D Show helices and sheets RCSB PDB PDBe
5IMW contains 34 α-helices and 67 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 | 58-70 | 13 | |
| α-helix | 75-78 | 4 | |
| β-strand | 80-82 | 3 | 1 |
| β-strand | 85-86 | 2 | 2 |
| β-strand | 91 | 1 | 1 |
| β-strand | 94 | 1 | 1 |
| β-strand | 97 | 1 | 1 |
| β-strand | 100-115 | 16 | 1 |
| β-strand | 118-119 | 2 | 3 |
| β-strand | 133-135 | 3 | 3 |
| α-helix | 138-141 | 4 | |
| β-strand | 147 | 1 | 3 |
| β-strand | 155-159 | 5 | 3 |
| α-helix | 166-169 | 4 | |
| β-strand | 170-173 | 4 | 3 |
| α-helix | 178-196 | 19 | |
| β-strand | 203 | 1 | 4 |
| α-helix | 204 | 1 | |
| β-strand | 205-212 | 8 | 3 |
| α-helix | 216-223 | 8 | |
| α-helix | 227-230 | 4 | |
| α-helix | 232-234 | 3 | |
| α-helix | 239-243 | 5 | |
| β-strand | 247-262 | 16 | 3 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-271 | 4 | |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 3 |
| α-helix | 317-324 | 8 | |
| β-strand | 344-350 | 7 | 3 |
| β-strand | 360-361 | 2 | 3 |
| α-helix | 366-374 | 9 | |
| β-strand | 377 | 1 | 4 |
| α-helix | 383-384 | 2 | |
| β-strand | 385-393 | 9 | 3 |
| β-strand | 399 | 1 | 3 |
| α-helix | 400-401 | 2 | |
| β-strand | 402-417 | 16 | 1 |
| β-strand | 421-425 | 5 | 5 |
| β-strand | 431-442 | 12 | 6 |
| β-strand | 448-454 | 7 | 6 |
| β-strand | 461-462 | 2 | 6 |
| β-strand | 466-470 | 5 | 5 |
| β-strand | 476-485 | 10 | 6 |
| β-strand | 495-500 | 6 | 6 |
| β-strand | 509-515 | 7 | 5 |
| β-strand | 520-526 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 58-69 | 12 | |
| β-strand | 80-82 | 3 | 7 |
| β-strand | 85-86 | 2 | 6 |
| β-strand | 91 | 1 | 8 |
| β-strand | 94-97 | 4 | 9 |
| β-strand | 100-105 | 6 | 9 |
| β-strand | 106 | 1 | 8 |
| β-strand | 108-115 | 8 | 7 |
| β-strand | 118-119 | 2 | 10 |
| α-helix | 125-127 | 3 | |
| β-strand | 133-135 | 3 | 10 |
| α-helix | 138-141 | 4 | |
| β-strand | 147 | 1 | 10 |
| β-strand | 155 | 1 | 11 |
| β-strand | 157-159 | 3 | 10 |
| β-strand | 170 | 1 | 10 |
| β-strand | 173 | 1 | 11 |
| α-helix | 178-196 | 19 | |
| β-strand | 203 | 1 | 12 |
| α-helix | 204 | 1 | |
| β-strand | 205-212 | 8 | 10 |
| α-helix | 216-223 | 8 | |
| α-helix | 227-231 | 5 | |
| α-helix | 232-234 | 3 | |
| α-helix | 239-243 | 5 | |
| β-strand | 247-262 | 16 | 10 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-271 | 4 | |
| α-helix | 279-283 | 5 | |
| β-strand | 287 | 1 | 13 |
| β-strand | 290 | 1 | 13 |
| β-strand | 292-310 | 19 | 10 |
| α-helix | 317-324 | 8 | |
| β-strand | 344-350 | 7 | 10 |
| α-helix | 352-353 | 2 | |
| β-strand | 359-361 | 3 | 10 |
| α-helix | 366-374 | 9 | |
| β-strand | 377 | 1 | 12 |
| α-helix | 383-384 | 2 | |
| β-strand | 385-393 | 9 | 10 |
| β-strand | 399 | 1 | 10 |
| β-strand | 402-409 | 8 | 7 |
| β-strand | 412-417 | 6 | 9 |
| β-strand | 419-425 | 7 | 14 |
| β-strand | 431 | 1 | 15 |
| β-strand | 432-442 | 11 | 2 |
| α-helix | 447 | 1 | |
| β-strand | 448-454 | 7 | 2 |
| β-strand | 462 | 1 | 15 |
| β-strand | 466-472 | 7 | 14 |
| β-strand | 476-484 | 9 | 2 |
| β-strand | 498-500 | 3 | 2 |
| β-strand | 509-515 | 7 | 14 |
| β-strand | 520-526 | 7 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Intermedilysin | A, B | protein | 471 | Streptococcus intermedius | Q9LCB8 (AlphaFold model) |
>5IMW_1 Intermedilysin (chains A, B) SEAAKKALNDYIWGLQYDKLNILTHQGEKLKNHSSREAFHRPGEYVVIEKKKQSISNATS KLSVSSANDDRIFPGALLKADQSLLENLPTLIPVNRGKTTISVNLPGLKNGESNLTVENP SNSTVRTAVNNLVEKWIQKYSKTHAVPARMQYESISAQSMSQLQAKFGADFSKVGAPLNV DFSSVHKGEKQVFIANFRQVYYTASVDSPNSPSALFGSGITPTDLINRGVNSKTPPVYVS NVSYGRAMYVKFETTSKSTKVQAAIDAVVKGAKLKAGTEYENILKNTKICAVVLGGNPGE ASKVCTGNIDTLKDLIQKGSNFSAQSPAVPISYTTSFVKDNSIATIQNNTDYIETKVTSY KDGALTLNHDGAFVARFYVYWEELGHDADGYETIRSRSWSGNGYNRGAHYSTTLRFKGNV RNIRVKVLGATGLAWEPWRLIYSKNDLPLVPQRNISTWGTTLHPQFEDKVV
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
Other PDB entries of the same protein (UniProt Q9LCB8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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