1XTC: Cholera toxin
Cholera toxin. Determined by X-ray diffraction at 2.4 Å resolution. Released 1 Aug 1996.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organism
- Vibrio cholerae
- Chains
- 7
- Atoms
- 6,135
- Mol. weight
- 85.71 kDa
- Released
- 1 Aug 1996
Explore 1XTC in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1XTC contains 30 α-helices and 46 β-strands across 7 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: 11 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-9 | 4 | 1 |
| α-helix | 13-19 | 7 | |
| β-strand | 21-22 | 2 | 2 |
| α-helix | 41-45 | 5 | |
| β-strand | 59-63 | 5 | 1 |
| α-helix | 67-71 | 5 | |
| β-strand | 78 | 1 | 3 |
| β-strand | 80 | 1 | 3 |
| β-strand | 83-88 | 6 | 1 |
| β-strand | 94-96 | 3 | 1 |
| α-helix | 97-101 | 5 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-110 | 3 | |
| β-strand | 112-116 | 5 | 1 |
| β-strand | 119-120 | 2 | 2 |
| β-strand | 124-130 | 7 | 1 |
| β-strand | 135-141 | 7 | 1 |
| α-helix | 147-150 | 4 | |
| α-helix | 158-160 | 3 | |
| α-helix | 172-175 | 4 | |
| α-helix | 179-181 | 3 | |
| α-helix | 183-184 | 2 | |
Chain C: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 197-233 | 37 | |
| α-helix | 236-239 | 4 | |
Chain D: 2 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-10 | 6 | |
| β-strand | 15-19 | 5 | 4 |
| β-strand | 26-29 | 4 | 5 |
| β-strand | 38-41 | 4 | 5 |
| β-strand | 48-50 | 3 | 5 |
| α-helix | 59-76 | 18 | |
| β-strand | 82-88 | 7 | 4 |
| β-strand | 96-102 | 7 | 4 |
Chain E: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| β-strand | 19 | 1 | 6 |
| β-strand | 24-30 | 7 | 4 |
| β-strand | 38-42 | 5 | 4 |
| β-strand | 47-50 | 4 | 4 |
| α-helix | 59-76 | 18 | |
| β-strand | 82 | 1 | 5 |
| β-strand | 84 | 1 | 6 |
| β-strand | 87-88 | 2 | 4 |
| β-strand | 94-96 | 3 | 4 |
| β-strand | 100-102 | 3 | 5 |
Chain F: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-8 | 4 | |
| β-strand | 15-23 | 9 | 4 |
| β-strand | 26-30 | 5 | 4 |
| β-strand | 32 | 1 | 7 |
| β-strand | 35 | 1 | 7 |
| β-strand | 38-41 | 4 | 4 |
| β-strand | 47-50 | 4 | 4 |
| α-helix | 51-52 | 2 | |
| α-helix | 59-62 | 4 | |
| α-helix | 64-77 | 14 | |
| β-strand | 81-88 | 8 | 4 |
| β-strand | 94-100 | 7 | 4 |
Chain G: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-22 | 8 | 4 |
| β-strand | 26-30 | 5 | 4 |
| β-strand | 38-40 | 3 | 4 |
| β-strand | 48-50 | 3 | 4 |
| α-helix | 51-52 | 2 | |
| α-helix | 60-66 | 7 | |
| α-helix | 69-77 | 9 | |
| β-strand | 82-88 | 7 | 4 |
| β-strand | 94-102 | 9 | 4 |
Chain H: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-22 | 8 | 4 |
| β-strand | 26-30 | 5 | 4 |
| β-strand | 38-41 | 4 | 4 |
| β-strand | 47-50 | 4 | 4 |
| α-helix | 51-53 | 3 | |
| α-helix | 59-61 | 3 | |
| α-helix | 62-67 | 6 | |
| α-helix | 69-77 | 9 | |
| β-strand | 82-88 | 7 | 4 |
| β-strand | 95-102 | 8 | 4 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Cholera toxin | A | protein | 194 | Vibrio cholerae | P01555 (AlphaFold model) |
| Cholera toxin | C | protein | 46 | Vibrio cholerae | P01555 (AlphaFold model) |
| Cholera toxin | D, E, F, G, H | protein | 103 | Vibrio cholerae | P01556 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>1XTC_1 CHOLERA TOXIN (chains A)
NDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYV
STSISLRSAHLVGQTILSGHSTYYLYVLATAPNMFNVNDVLGAYSPHPDEQEVSALGGIP
YSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWI
HHAPPGCGNAPRSS
Sequence of entity 2 (C), FASTA
>1XTC_2 CHOLERA TOXIN (chains C)
MSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL
Sequence of entity 3 (D, E, F, G, H), FASTA
>1XTC_3 CHOLERA TOXIN (chains D, E, F, G, H)
TPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPSSQHIDS
QKKAIERMKDTLRIAYLTEAKVEKLCTWNNKTPHAIAAISMAN
Primary citation
The three-dimensional crystal structure of cholera toxin. Zhang, R.G., Scott, D.L., Westbrook, M.L. et al. J Mol Biol (1995) 251:563-573. DOI 10.1006/jmbi.1995.0456 · PubMed
Other PDB entries of the same protein (UniProt P01555 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8OXS 1.6 Å, Cholera holotoxin variant (chimera with E. coli heat-labile enterotoxin, 4 C-terminal…
- 8Q6I 1.6 Å, Cholera holotoxin variant (chimera with E. coli heat-labile enterotoxin, 1 C-terminal…
- 1S5D 1.75 Å, Cholera holotoxin with an A-subunit Y30S mutation, Crystal form 2
- 2A5D 1.8 Å, Structural basis for the activation of cholera toxin by human ARF6-GTP
- 1S5E 1.9 Å, Cholera holotoxin, Crystal form 1
- 2A5F 2.02 Å, Cholera toxin A1 subunit bound to its substrate, NAD+, and its human protein activator,…
- 1S5B 2.13 Å, Cholera holotoxin with an A-subunit Y30S mutation Form 3
- 8QRE 2.3 Å, Cholera holotoxin (wildtype)
- 1S5C 2.5 Å, Cholera holotoxin with an A-subunit Y30S mutation, Crystal form 1
- 1S5F 2.6 Å, Cholera holotoxin, Crystal form 2
- 2A5G 2.66 Å, Cholera toxin A1 subunit bound to ARF6(Q67L)
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