Structure of a disulfide locked mutant of Intermedilysin with human CD59. Determined by X-ray diffraction at 3.49 Å resolution. Released 8 May 2013.
Explore 4BIK in 3D Show helices and sheets RCSB PDB PDBe
4BIK contains 48 α-helices and 62 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 | 57-70 | 14 | |
| α-helix | 75-78 | 4 | |
| β-strand | 80-82 | 3 | 1 |
| β-strand | 90-97 | 8 | 1 |
| β-strand | 100-115 | 16 | 1 |
| β-strand | 118-119 | 2 | 2 |
| α-helix | 120 | 1 | |
| α-helix | 125-127 | 3 | |
| β-strand | 133-135 | 3 | 2 |
| α-helix | 138-141 | 4 | |
| α-helix | 145-146 | 2 | |
| β-strand | 147 | 1 | 2 |
| α-helix | 151 | 1 | |
| β-strand | 152 | 1 | 3 |
| α-helix | 153-154 | 2 | |
| β-strand | 155-159 | 5 | 2 |
| β-strand | 170-173 | 4 | 2 |
| α-helix | 178-194 | 17 | |
| α-helix | 196-198 | 3 | |
| β-strand | 205-212 | 8 | 2 |
| α-helix | 216-223 | 8 | |
| α-helix | 227-230 | 4 | |
| α-helix | 238-242 | 5 | |
| β-strand | 247-262 | 16 | 2 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-271 | 4 | |
| β-strand | 272 | 1 | 3 |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 2 |
| α-helix | 318-325 | 8 | |
| α-helix | 336-341 | 6 | |
| β-strand | 343-349 | 7 | 2 |
| β-strand | 361-362 | 2 | 2 |
| α-helix | 366-374 | 9 | |
| α-helix | 383-384 | 2 | |
| β-strand | 385-393 | 9 | 2 |
| α-helix | 398 | 1 | |
| β-strand | 399 | 1 | 2 |
| α-helix | 400 | 1 | |
| β-strand | 402-417 | 16 | 1 |
| β-strand | 419-425 | 7 | 4 |
| β-strand | 432-443 | 12 | 5 |
| β-strand | 447-454 | 8 | 5 |
| β-strand | 466-472 | 7 | 4 |
| β-strand | 476-486 | 11 | 5 |
| β-strand | 494-503 | 10 | 5 |
| β-strand | 509-515 | 7 | 4 |
| β-strand | 520-522 | 3 | 4 |
| β-strand | 525-526 | 2 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 6 |
| β-strand | 16-18 | 3 | 6 |
| β-strand | 25-31 | 7 | 5 |
| β-strand | 34-40 | 7 | 5 |
| α-helix | 42-44 | 3 | |
| α-helix | 47-54 | 8 | |
| β-strand | 60-64 | 5 | 5 |
| α-helix | 72-74 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 58-70 | 13 | |
| β-strand | 80-82 | 3 | 7 |
| β-strand | 90-97 | 8 | 7 |
| β-strand | 100-115 | 16 | 7 |
| β-strand | 118-119 | 2 | 8 |
| α-helix | 120 | 1 | |
| α-helix | 125-127 | 3 | |
| β-strand | 133-135 | 3 | 8 |
| α-helix | 138-141 | 4 | |
| α-helix | 145-146 | 2 | |
| β-strand | 147 | 1 | 8 |
| α-helix | 151-154 | 4 | |
| β-strand | 155-159 | 5 | 8 |
| α-helix | 166-168 | 3 | |
| β-strand | 170-173 | 4 | 8 |
| α-helix | 178-194 | 17 | |
| α-helix | 196-198 | 3 | |
| β-strand | 205-212 | 8 | 8 |
| α-helix | 216-223 | 8 | |
| α-helix | 227-230 | 4 | |
| α-helix | 238-242 | 5 | |
| β-strand | 247-262 | 16 | 8 |
| α-helix | 263-265 | 3 | |
| α-helix | 268-271 | 4 | |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 8 |
| α-helix | 318-325 | 8 | |
| α-helix | 337-341 | 5 | |
| β-strand | 344-349 | 6 | 8 |
| α-helix | 366-374 | 9 | |
| α-helix | 383-384 | 2 | |
| β-strand | 385-393 | 9 | 8 |
| α-helix | 398 | 1 | |
| β-strand | 399-400 | 2 | 8 |
| β-strand | 402-417 | 16 | 7 |
| β-strand | 419-425 | 7 | 9 |
| β-strand | 431 | 1 | 10 |
| β-strand | 432-443 | 12 | 11 |
| β-strand | 447-454 | 8 | 11 |
| β-strand | 462 | 1 | 10 |
| β-strand | 466-472 | 7 | 9 |
| β-strand | 476-486 | 11 | 11 |
| β-strand | 494-503 | 10 | 11 |
| β-strand | 509-515 | 7 | 9 |
| β-strand | 520-526 | 7 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Intermedilysin | A, C | protein | 535 | STREPTOCOCCUS INTERMEDIUS | Q9LCB8 (AlphaFold model) |
| CD59 glycoprotein | B, D | protein | 79 | HOMO SAPIENS | P13987 (AlphaFold model) |
>4BIK_1 INTERMEDILYSIN (chains A, C) MGGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSETPTKPKAAQTEKKTEKKPENSNS EAAKKALNDYIWGLQYDKLNILTHQGEKLKNHSSREAFHRPGEYVVIEKKKQSISNATSK LSVSSANDDRIFPGALLKADQSLLENLPTLIPVNRGKTTISVNLPGLKNGESNLTVENPS NSTVRTAVNNLVEKWIQNYSKTHAVPARMQYESISAQSMSQLQAKFGADFSKVGAPLNVD FSSVHKGEKQVFIANFRQVYYTASVDSPNSPSALFGSGITPTDLINRGVNSKTPPVYVSN VSYGRAMYVKFETTSKSTKVQAAIDAVVKGAKLKAGTEYENILKNTKICAVVLGGNPGEA SKVCTGNIDTLKDLIQKGSNFSAQSPAVPISYTTSFVKDNSIATIQNNTDYIETKVTSYK DGALTLNHDGAFVARFYVYWEELGHDADGYETIRSRSWSGNGYNRGAHYSTTLRFKGNVR NIRVKVLGATGLAWEPWRLIYSKNDLPLVPQRNISTWGTTLHPQFEDKVVKDNTD
>4BIK_2 CD59 GLYCOPROTEIN (chains B, D) MLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENEL TYYCCKKDLCNFNEQLENC
Structural Basis for Recognition of the Pore- Forming Toxin Intermedilysin by Human Complement Receptor Cd59. Johnson, S., Brooks, N.J., Smith, R.A.G. et al. Cell Rep (2013) 3:1369. DOI 10.1016/J.CELREP.2013.04.029 · 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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