1KTK: Exotoxin type C
Complex of Streptococcal pyrogenic enterotoxin C (SpeC) with a human T cell receptor beta chain (Vbeta2.1). Determined by X-ray diffraction at 3.0 Å resolution. Released 7 Jun 2002.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organisms
- Streptococcus pyogenes, Homo sapiens
- Chains
- 6
- Atoms
- 9,511
- Mol. weight
- 152.46 kDa
- Released
- 7 Jun 2002
Explore 1KTK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1KTK contains 32 α-helices and 105 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: 7 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-17 | 11 | |
| α-helix | 20-21 | 2 | |
| β-strand | 22-32 | 11 | 1 |
| β-strand | 36-40 | 5 | 1 |
| β-strand | 50-54 | 5 | 1 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 83-86 | 4 | 1 |
| β-strand | 90-92 | 3 | 1 |
| β-strand | 100-101 | 2 | 2 |
| α-helix | 102 | 1 | |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 114 | 1 | 3 |
| β-strand | 121-122 | 2 | 2 |
| β-strand | 126-128 | 3 | 4 |
| α-helix | 129-144 | 16 | |
| β-strand | 155-162 | 8 | 3 |
| β-strand | 168-171 | 4 | 3 |
| α-helix | 181-184 | 4 | |
| α-helix | 185-190 | 6 | |
| β-strand | 193-195 | 3 | 4 |
| α-helix | 196-198 | 3 | |
| β-strand | 199-207 | 9 | 3 |
Chain B: 7 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-13 | 8 | |
| β-strand | 22 | 1 | 5 |
| β-strand | 27 | 1 | 6 |
| β-strand | 28-32 | 5 | 7 |
| β-strand | 36-40 | 5 | 7 |
| β-strand | 50-54 | 5 | 7 |
| β-strand | 69-70 | 2 | 6 |
| β-strand | 73 | 1 | 5 |
| β-strand | 83-86 | 4 | 7 |
| β-strand | 91-92 | 2 | 6 |
| α-helix | 93-94 | 2 | |
| β-strand | 100-101 | 2 | 8 |
| α-helix | 102-103 | 2 | |
| β-strand | 104-107 | 4 | 9 |
| β-strand | 115 | 1 | 9 |
| β-strand | 121-122 | 2 | 8 |
| β-strand | 126 | 1 | 10 |
| α-helix | 129-144 | 16 | |
| β-strand | 156-162 | 7 | 9 |
| β-strand | 167-171 | 5 | 9 |
| α-helix | 181-185 | 5 | |
| α-helix | 186-188 | 3 | |
| β-strand | 195 | 1 | 10 |
| α-helix | 196-198 | 3 | |
| β-strand | 199-206 | 8 | 9 |
Chain C: 8 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-17 | 6 | |
| α-helix | 20-21 | 2 | |
| β-strand | 22 | 1 | 11 |
| β-strand | 27-28 | 2 | 12 |
| β-strand | 29-32 | 4 | 13 |
| β-strand | 36-40 | 5 | 13 |
| α-helix | 42-45 | 4 | |
| β-strand | 50-54 | 5 | 13 |
| α-helix | 57-60 | 4 | |
| β-strand | 68-71 | 4 | 12 |
| β-strand | 73 | 1 | 11 |
| β-strand | 75-77 | 3 | 13 |
| β-strand | 83-86 | 4 | 13 |
| β-strand | 90-92 | 3 | 12 |
| α-helix | 93-94 | 2 | |
| β-strand | 100-101 | 2 | 14 |
| β-strand | 104-108 | 5 | 15 |
| β-strand | 114-115 | 2 | 15 |
| β-strand | 121-122 | 2 | 14 |
| β-strand | 126-128 | 3 | 16 |
| α-helix | 129-144 | 16 | |
| β-strand | 157-162 | 6 | 15 |
| β-strand | 168-171 | 4 | 15 |
| α-helix | 181-184 | 4 | |
| α-helix | 185-188 | 4 | |
| β-strand | 193-195 | 3 | 16 |
| β-strand | 199-206 | 8 | 15 |
Chain D: 9 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-16 | 8 | |
| α-helix | 20-21 | 2 | |
| β-strand | 22 | 1 | 17 |
| β-strand | 27 | 1 | 18 |
| β-strand | 29-32 | 4 | 19 |
| β-strand | 37-40 | 4 | 19 |
| β-strand | 50-53 | 4 | 19 |
| α-helix | 57-60 | 4 | |
| β-strand | 69-71 | 3 | 18 |
| β-strand | 73 | 1 | 17 |
| β-strand | 75 | 1 | 19 |
| β-strand | 83-86 | 4 | 19 |
| β-strand | 90-92 | 3 | 18 |
| α-helix | 93-94 | 2 | |
| β-strand | 100-101 | 2 | 20 |
| α-helix | 102 | 1 | |
| β-strand | 103-108 | 6 | 21 |
| β-strand | 109 | 1 | 22 |
| β-strand | 111 | 1 | 22 |
| β-strand | 121-122 | 2 | 20 |
| β-strand | 126-128 | 3 | 23 |
| α-helix | 129-139 | 11 | |
| β-strand | 155-161 | 7 | 21 |
| β-strand | 168-171 | 4 | 21 |
| α-helix | 181-184 | 4 | |
| α-helix | 185-188 | 4 | |
| β-strand | 193-195 | 3 | 23 |
| α-helix | 196-198 | 3 | |
| β-strand | 201-207 | 7 | 21 |
Chain E: 1 helix, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-6 | 3 | 24 |
| β-strand | 20-25 | 6 | 24 |
| β-strand | 32-36 | 5 | 25 |
| β-strand | 44-49 | 6 | 25 |
| β-strand | 55-57 | 3 | 25 |
| β-strand | 66-71 | 6 | 24 |
| β-strand | 74-78 | 5 | 24 |
| β-strand | 89-91 | 3 | 25 |
| β-strand | 112-113 | 2 | 25 |
| β-strand | 126-130 | 5 | 26 |
| β-strand | 142-143 | 2 | 27 |
| β-strand | 146-150 | 5 | 26 |
| β-strand | 161-163 | 3 | 28 |
| β-strand | 166-167 | 2 | 28 |
| β-strand | 173-174 | 2 | 26 |
| α-helix | 178 | 1 | |
| β-strand | 179-180 | 2 | 26 |
| β-strand | 190-195 | 6 | 26 |
| β-strand | 198-199 | 2 | 27 |
| β-strand | 209-214 | 6 | 28 |
| β-strand | 237-242 | 6 | 28 |
Chain F: 0 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-6 | 2 | 29 |
| β-strand | 18 | 1 | 30 |
| β-strand | 22 | 1 | 31 |
| β-strand | 23-24 | 2 | 29 |
| β-strand | 33 | 1 | 32 |
| β-strand | 48 | 1 | 32 |
| β-strand | 65-69 | 5 | 31 |
| β-strand | 75-79 | 5 | 31 |
| β-strand | 80 | 1 | 30 |
| β-strand | 90 | 1 | 33 |
| β-strand | 112 | 1 | 33 |
| β-strand | 149-150 | 2 | 34 |
| β-strand | 191-192 | 2 | 34 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Exotoxin type C | A, B, C, D | protein | 208 | Streptococcus pyogenes | Q8NKX2 (AlphaFold model) |
| T-cell receptor beta chain | E, F | protein | 247 | Homo sapiens | P01850 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>1KTK_1 Exotoxin type C (chains A, B, C, D)
DSKKDISNVKSDLLYAYTITPYDYKDCRVNFSTTHTLNIDTQKYRGKDYYISSEMSYEAS
QKFKRDDHVDVFGLFYILNSHTGEYIYGGITPAQNNKVNHKLLGNLFISGESQQNLNNKI
ILEKDIVTFQEIDFKIRKYLMDNYKIYDATSPYVSGRIEIGTKDGKHEQIDLFDSPNEGT
RSDIFAKYKDNRIINMKNFSHFDIYLEK
Sequence of entity 2 (E, F), FASTA
>1KTK_2 T-cell receptor beta chain (chains E, F)
GAVVSQHPSRVIAKSGTSVKIECRSLDFQATTMFWYRQFPKQSLMLMATSAEGSKATYEQ
GVEKDKFLINHASLTLSTLTVTSAHPEDSSFYICSALAGSGSSTDTQYFGPGTRLTVLED
LKNFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPL
KEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSA
EAWGRAD
Primary citation
Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes. Sundberg, E.J., Li, H., Llera, A.S. et al. Structure (2002) 10:687-699. DOI 10.1016/S0969-2126(02)00759-1 · PubMed
Other PDB entries of the same protein (UniProt Q8NKX2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1AN8 2.4 Å, Crystal structure of the streptococcal superantigen spe-C
- 1HQR 3.2 Å, Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on…
Browse structure collections
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