6ZD0: Thiol-activated cytolysin
Disulfide-locked early prepore intermedilysin-CD59. Determined by electron microscopy at 4.6 Å resolution. Released 18 Nov 2020.
- Method
- Electron microscopy
- Resolution
- 4.6 Å
- Organisms
- Streptococcus intermedius, Homo sapiens
- Chains
- 6
- Atoms
- 7,962
- Mol. weight
- 204.92 kDa
- Released
- 18 Nov 2020
Explore 6ZD0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6ZD0 contains 58 α-helices and 98 β-strands across 6 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.
Chain A: 19 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 57-68 | 12 | |
| α-helix | 75-78 | 4 | |
| β-strand | 81-84 | 4 | 1 |
| β-strand | 91-97 | 7 | 1 |
| β-strand | 100-112 | 13 | 1 |
| β-strand | 115 | 1 | 2 |
| β-strand | 118-119 | 2 | 3 |
| α-helix | 122-124 | 3 | |
| β-strand | 133-135 | 3 | 3 |
| α-helix | 138-141 | 4 | |
| α-helix | 150-151 | 2 | |
| β-strand | 152 | 1 | 4 |
| β-strand | 155-160 | 6 | 3 |
| β-strand | 170-173 | 4 | 3 |
| α-helix | 178-195 | 18 | |
| α-helix | 197-199 | 3 | |
| β-strand | 208-212 | 5 | 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 | 268-270 | 3 | |
| β-strand | 272 | 1 | 4 |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 3 |
| α-helix | 316-324 | 9 | |
| α-helix | 336-341 | 6 | |
| β-strand | 348 | 1 | 3 |
| α-helix | 359-362 | 4 | |
| α-helix | 365-371 | 7 | |
| α-helix | 379 | 1 | |
| β-strand | 385-393 | 9 | 3 |
| β-strand | 398-399 | 2 | 3 |
| α-helix | 400 | 1 | |
| β-strand | 402 | 1 | 2 |
| β-strand | 404-411 | 8 | 1 |
| β-strand | 414-417 | 4 | 1 |
| β-strand | 420-425 | 6 | 5 |
| β-strand | 431-442 | 12 | 6 |
| β-strand | 448-453 | 6 | 6 |
| β-strand | 467-470 | 4 | 5 |
| β-strand | 476-486 | 11 | 6 |
| β-strand | 494-503 | 10 | 6 |
| β-strand | 508-515 | 8 | 5 |
| β-strand | 520-525 | 6 | 5 |
Chain B: 1 helix, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 7 |
| β-strand | 16-18 | 3 | 7 |
| β-strand | 23 | 1 | 6 |
| β-strand | 25-31 | 7 | 6 |
| β-strand | 34-40 | 7 | 6 |
| α-helix | 47-53 | 7 | |
| β-strand | 60-64 | 5 | 6 |
Chain C: 17 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 57-70 | 14 | |
| α-helix | 75-78 | 4 | |
| β-strand | 80-82 | 3 | 8 |
| β-strand | 90-97 | 8 | 9 |
| β-strand | 100-107 | 8 | 9 |
| β-strand | 108-111 | 4 | 10 |
| β-strand | 115 | 1 | 11 |
| β-strand | 118-119 | 2 | 12 |
| α-helix | 122-127 | 6 | |
| β-strand | 133-135 | 3 | 12 |
| α-helix | 138-141 | 4 | |
| β-strand | 155-159 | 5 | 12 |
| β-strand | 170-173 | 4 | 12 |
| α-helix | 178-195 | 18 | |
| α-helix | 197-199 | 3 | |
| β-strand | 208-212 | 5 | 12 |
| 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 | 12 |
| α-helix | 268-271 | 4 | |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 12 |
| α-helix | 316-324 | 9 | |
| α-helix | 336-341 | 6 | |
| β-strand | 348 | 1 | 12 |
| α-helix | 358-362 | 5 | |
| α-helix | 367-370 | 4 | |
| α-helix | 371-376 | 6 | |
| β-strand | 385 | 1 | 12 |
| β-strand | 388-393 | 6 | 12 |
| β-strand | 399 | 1 | 12 |
| β-strand | 402 | 1 | 11 |
| β-strand | 403-405 | 3 | 8 |
| β-strand | 406-409 | 4 | 10 |
| β-strand | 415-417 | 3 | 9 |
| β-strand | 420-423 | 4 | 13 |
| β-strand | 431-443 | 13 | 14 |
| β-strand | 447-453 | 7 | 14 |
| β-strand | 468-470 | 3 | 13 |
| β-strand | 476-485 | 10 | 14 |
| β-strand | 496-503 | 8 | 14 |
| β-strand | 508-516 | 9 | 13 |
| β-strand | 519-525 | 7 | 13 |
Chain D: 2 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 15 |
| β-strand | 16-18 | 3 | 15 |
| β-strand | 25-31 | 7 | 14 |
| β-strand | 34-40 | 7 | 14 |
| α-helix | 47-53 | 7 | |
| β-strand | 60-64 | 5 | 14 |
| α-helix | 72-74 | 3 | |
Chain E: 16 helices, 26 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 57-70 | 14 | |
| α-helix | 75-78 | 4 | |
| β-strand | 81-82 | 2 | 16 |
| β-strand | 91-97 | 7 | 16 |
| β-strand | 100-113 | 14 | 16 |
| β-strand | 118-119 | 2 | 17 |
| α-helix | 122-127 | 6 | |
| β-strand | 134-135 | 2 | 17 |
| α-helix | 138-141 | 4 | |
| β-strand | 152 | 1 | 18 |
| β-strand | 155-160 | 6 | 17 |
| β-strand | 170-173 | 4 | 17 |
| α-helix | 178-195 | 18 | |
| α-helix | 197-199 | 3 | |
| β-strand | 209-212 | 4 | 17 |
| α-helix | 217-221 | 5 | |
| α-helix | 227-230 | 4 | |
| α-helix | 238-242 | 5 | |
| β-strand | 247-262 | 16 | 17 |
| β-strand | 272 | 1 | 18 |
| α-helix | 278-283 | 6 | |
| β-strand | 292-310 | 19 | 17 |
| α-helix | 317-323 | 7 | |
| α-helix | 336-341 | 6 | |
| β-strand | 346-348 | 3 | 17 |
| α-helix | 357-362 | 6 | |
| α-helix | 367-373 | 7 | |
| β-strand | 386-393 | 8 | 17 |
| α-helix | 398 | 1 | |
| β-strand | 399 | 1 | 17 |
| α-helix | 400 | 1 | |
| β-strand | 404-413 | 10 | 16 |
| β-strand | 416 | 1 | 16 |
| β-strand | 419-425 | 7 | 19 |
| β-strand | 432-441 | 10 | 20 |
| β-strand | 449-454 | 6 | 20 |
| β-strand | 460-461 | 2 | 20 |
| β-strand | 466-472 | 7 | 19 |
| β-strand | 476-486 | 11 | 20 |
| β-strand | 494-503 | 10 | 20 |
| β-strand | 509-516 | 8 | 19 |
| β-strand | 519-526 | 8 | 19 |
Chain F: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 21 |
| β-strand | 8 | 1 | 20 |
| β-strand | 16-18 | 3 | 21 |
| β-strand | 25-31 | 7 | 20 |
| β-strand | 34-40 | 7 | 20 |
| α-helix | 42-44 | 3 | |
| α-helix | 47-54 | 8 | |
| β-strand | 60-64 | 5 | 20 |
| α-helix | 72-74 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Thiol-activated cytolysin | A, C, E | protein | 535 | Streptococcus intermedius | Q9LCB8 (AlphaFold model) |
| CD59 glycoprotein | B, D, F | protein | 79 | Homo sapiens | P13987 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>6ZD0_1 Thiol-activated cytolysin (chains A, C, E)
MGGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSETPTKPKAAQTEKKTEKKPENSNS
EAAKKALNDYIWGLQYDKLNILTHQGEKLKNHSSREAFHRPGEYVVCEKKKQSISNATSK
LSVSSANDDRIFPGALLKADQSLLENLPTLIPVNRGKTTISVNLPGLKNGESNLTVENPS
NSTVRTAVNNLVEKWIQNYSKTHAVPARMQYESISAQSMSQLQAKFGADFSKVGAPLNVD
FSSVHKCEKQVFIANFRQVYYTASVDSPNSPSALFGSGITPTDLINRGVNSKTPPVYVSN
VSYGRAMYVKFETTSKSTKVQAAIDAVVKGAKLKAGTEYENILKNTKITAVVLGGNPGEA
SKVITGNIDTLKDLIQKGSNFSAQSPAVPISYTTSFVKDNSIATIQNNTDYIETKVTSYK
DGALTLNHDGAFVARFYVYWEELGHDADGYETIRSRSWSGNGYNRGAHYSTTLRFKGNVR
NIRVKVLGATGLAWEPWRLIYSKNDLPLVPQRNISTWGTTLHPQFEDKVVKDNTD
Sequence of entity 2 (B, D, F), FASTA
>6ZD0_2 CD59 glycoprotein (chains B, D, F)
MLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENEL
TYYCCKKDLCNFNEQLENC
Primary citation
Structural basis for tuning activity and membrane specificity of bacterial cytolysins. Shah, N.R., Voisin, T.B., Parsons, E.S. et al. Nat Commun (2020) 11:5818-5818. DOI 10.1038/s41467-020-19482-6 · PubMed
Other PDB entries of the same protein (UniProt Q9LCB8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1S3R 2.6 Å, Crystal structure of the human-specific toxin intermedilysin
- 5IMT 2.7 Å, Toxin receptor complex
- 5IMW 2.89 Å, Trapped Toxin
- 4BIK 3.49 Å, Structure of a disulfide locked mutant of Intermedilysin with human CD59
Browse structure collections
About this viewer
MolViewer shows 6ZD0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.