Crystal structure of the human-specific toxin intermedilysin. Determined by X-ray diffraction at 2.6 Å resolution. Released 25 Jan 2005.
Explore 1S3R in 3D Show helices and sheets RCSB PDB PDBe
1S3R contains 43 α-helices and 62 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 | 57-69 | 13 | |
| β-strand | 80-82 | 3 | 1 |
| β-strand | 85-86 | 2 | 2 |
| β-strand | 90-97 | 8 | 1 |
| β-strand | 100-115 | 16 | 1 |
| β-strand | 118-119 | 2 | 3 |
| α-helix | 120 | 1 | |
| α-helix | 125-127 | 3 | |
| β-strand | 133-135 | 3 | 3 |
| α-helix | 138-141 | 4 | |
| α-helix | 145-146 | 2 | |
| β-strand | 147 | 1 | 3 |
| α-helix | 148 | 1 | |
| β-strand | 152 | 1 | 4 |
| β-strand | 155-159 | 5 | 3 |
| β-strand | 170-173 | 4 | 3 |
| α-helix | 178-192 | 15 | |
| α-helix | 193-197 | 5 | |
| β-strand | 203 | 1 | 5 |
| 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 | 238-242 | 5 | |
| β-strand | 247-262 | 16 | 3 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-271 | 4 | |
| β-strand | 272 | 1 | 4 |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 3 |
| α-helix | 317-325 | 9 | |
| α-helix | 337-340 | 4 | |
| β-strand | 345-350 | 6 | 3 |
| β-strand | 360-363 | 4 | 3 |
| α-helix | 365-374 | 10 | |
| β-strand | 377 | 1 | 5 |
| α-helix | 383-384 | 2 | |
| β-strand | 385-393 | 9 | 3 |
| α-helix | 398 | 1 | |
| β-strand | 399 | 1 | 3 |
| α-helix | 400 | 1 | |
| β-strand | 402-417 | 16 | 1 |
| β-strand | 419-425 | 7 | 6 |
| β-strand | 431-442 | 12 | 7 |
| β-strand | 448-454 | 7 | 7 |
| β-strand | 462 | 1 | 7 |
| β-strand | 467-472 | 6 | 6 |
| β-strand | 476-486 | 11 | 7 |
| β-strand | 494-503 | 10 | 7 |
| β-strand | 508-515 | 8 | 6 |
| β-strand | 520-526 | 7 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 57-69 | 13 | |
| α-helix | 75-78 | 4 | |
| β-strand | 80-82 | 3 | 8 |
| β-strand | 86 | 1 | 7 |
| β-strand | 90-91 | 2 | 8 |
| β-strand | 94-97 | 4 | 8 |
| β-strand | 100-115 | 16 | 8 |
| β-strand | 118-119 | 2 | 9 |
| α-helix | 120 | 1 | |
| β-strand | 133-135 | 3 | 9 |
| α-helix | 138-141 | 4 | |
| α-helix | 145-146 | 2 | |
| β-strand | 147 | 1 | 9 |
| α-helix | 148 | 1 | |
| β-strand | 152 | 1 | 10 |
| β-strand | 155-159 | 5 | 9 |
| β-strand | 170-173 | 4 | 9 |
| α-helix | 178-196 | 19 | |
| β-strand | 203 | 1 | 11 |
| β-strand | 205-212 | 8 | 9 |
| α-helix | 216-223 | 8 | |
| α-helix | 227-230 | 4 | |
| α-helix | 232-234 | 3 | |
| α-helix | 238-242 | 5 | |
| β-strand | 247-262 | 16 | 9 |
| α-helix | 263 | 1 | |
| α-helix | 268-271 | 4 | |
| β-strand | 272 | 1 | 10 |
| α-helix | 273 | 1 | |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 9 |
| α-helix | 317-323 | 7 | |
| α-helix | 324-328 | 5 | |
| α-helix | 336-341 | 6 | |
| β-strand | 343-350 | 8 | 9 |
| β-strand | 361-363 | 3 | 9 |
| α-helix | 365-374 | 10 | |
| β-strand | 377 | 1 | 11 |
| β-strand | 385-393 | 9 | 9 |
| α-helix | 398 | 1 | |
| β-strand | 399 | 1 | 9 |
| α-helix | 400 | 1 | |
| β-strand | 402-417 | 16 | 8 |
| β-strand | 419-425 | 7 | 12 |
| β-strand | 431 | 1 | 13 |
| β-strand | 432-442 | 11 | 2 |
| β-strand | 448-454 | 7 | 2 |
| β-strand | 462 | 1 | 13 |
| β-strand | 467-472 | 6 | 12 |
| β-strand | 476-486 | 11 | 2 |
| β-strand | 494-500 | 7 | 2 |
| β-strand | 508-515 | 8 | 12 |
| β-strand | 520-526 | 7 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| intermedilysin | A, B | protein | 535 | Streptococcus intermedius | Q9LCB8 (AlphaFold model) |
>1S3R_1 intermedilysin (chains A, B) MGGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSETPTKPKAAQTEKKTEKKPENSNS EAAKKALNDYIWGLQYDKLNILTHQGEKLKNHSSREAFHRPGEYVVIEKKKQSISNATSK LSVSSANDDRIFPGALLKADQSLLENLPTLIPVNRGKTTISVNLPGLKNGESNLTVENPS NSTVRTAVNNLVEKWIQNYSKTHAVPARMQYESISAQSMSQLQAKFGADFSKVGAPLNVD FSSVHKGEKQVFIANFRQVYYTASVDSPNSPSALFGSGITPTDLINRGVNSKTPPVYVSN VSYGRAMYVKFETTSKSTKVQAAIDAVVKGAKLKAGTEYENILKNTKITAVVLGGNPGEA SKVITGNIDTLKDLIQKGSNFSAQSPAVPISYTTSFVKDNSIATIQNNTDYIETKVTSYK DGALTLNHDGAFVARFYVYWEELGHDADGYETIRSRSWSGNGYNRGAHYSTTLRFKGNVR NIRVKVLGATGLAWEPWRLIYSKNDLPLVPQRNISTWGTTLHPQFEDKVVKDNTD
Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin. Polekhina, G., Giddings, K.S., Tweten, R.K. et al. Proc Natl Acad Sci U S A (2005) 102:600-605. DOI 10.1073/pnas.0403229101 · 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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