1S5C: Cholera enterotoxin, A chain
Cholera holotoxin with an A-subunit Y30S mutation, Crystal form 1. Determined by X-ray diffraction at 2.5 Å resolution. Released 6 Apr 2004.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Vibrio cholerae
- Chains
- 6
- Atoms
- 5,707
- Mol. weight
- 85.29 kDa
- Released
- 6 Apr 2004
Explore 1S5C in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1S5C contains 31 α-helices and 43 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: 15 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-9 | 6 | 1 |
| α-helix | 13-19 | 7 | |
| β-strand | 21-22 | 2 | 2 |
| α-helix | 41-46 | 6 | |
| β-strand | 59-63 | 5 | 1 |
| α-helix | 66-76 | 11 | |
| β-strand | 82-89 | 8 | 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 |
| α-helix | 121-123 | 3 | |
| β-strand | 124-131 | 8 | 1 |
| β-strand | 134-135 | 2 | 1 |
| β-strand | 140-141 | 2 | 1 |
| α-helix | 147-151 | 5 | |
| α-helix | 155 | 1 | |
| β-strand | 156 | 1 | 1 |
| α-helix | 157 | 1 | |
| α-helix | 158-162 | 5 | |
| α-helix | 172-175 | 4 | |
| α-helix | 179-182 | 4 | |
| α-helix | 183-184 | 2 | |
| α-helix | 198-226 | 29 | |
Chain D: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-10 | 6 | |
| β-strand | 15-22 | 8 | 3 |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 37-41 | 5 | 3 |
| β-strand | 48-50 | 3 | 3 |
| α-helix | 51-52 | 2 | |
| α-helix | 60-78 | 19 | |
| β-strand | 82-88 | 7 | 3 |
| β-strand | 94-102 | 9 | 3 |
Chain E: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-22 | 8 | 3 |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 37-41 | 5 | 3 |
| β-strand | 47-50 | 4 | 3 |
| α-helix | 51-53 | 3 | |
| α-helix | 61-78 | 18 | |
| β-strand | 82-88 | 7 | 3 |
| β-strand | 94-102 | 9 | 3 |
Chain F: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-22 | 8 | 3 |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 32 | 1 | 4 |
| β-strand | 35 | 1 | 4 |
| β-strand | 38-41 | 4 | 3 |
| β-strand | 47-50 | 4 | 3 |
| α-helix | 51-52 | 2 | |
| α-helix | 59-78 | 20 | |
| β-strand | 82-88 | 7 | 3 |
| β-strand | 94-102 | 9 | 3 |
Chain G: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-23 | 9 | 3 |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 37-41 | 5 | 3 |
| β-strand | 47-50 | 4 | 3 |
| α-helix | 51-53 | 3 | |
| α-helix | 59-77 | 19 | |
| α-helix | 80 | 1 | |
| β-strand | 81-88 | 8 | 3 |
| β-strand | 94-102 | 9 | 3 |
Chain H: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-22 | 8 | 3 |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 38-41 | 4 | 3 |
| β-strand | 47-50 | 4 | 3 |
| α-helix | 51-53 | 3 | |
| α-helix | 62-78 | 17 | |
| β-strand | 82-88 | 7 | 3 |
| β-strand | 94-102 | 9 | 3 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Cholera enterotoxin, A chain | A | protein | 240 | Vibrio cholerae | P01555 (AlphaFold model) |
| cholera enterotoxin B-subunit | D, E, F, G, H | protein | 103 | Vibrio cholerae | P01556 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>1S5C_1 Cholera enterotoxin, A chain (chains A)
NDDKLYRADSRPPDEIKQSGGLMPRGQSESFDRGTQMNINLYDHARGTQTGFVRHDDGYV
STSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIP
YSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWI
HHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL
Sequence of entity 2 (D, E, F, G, H), FASTA
>1S5C_2 cholera enterotoxin B-subunit (chains D, E, F, G, H)
TPQNITDLCAEYHNTQIHTLNDKIFSYTESLAGKREMAIITFKNGATFQVEVPGSQHIDS
QKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN
Primary citation
Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. O'Neal, C.J., Amaya, E.I., Jobling, M.G. et al. Biochemistry (2004) 43:3772-3782. DOI 10.1021/bi0360152 · 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)
- 1XTC 2.4 Å, Cholera toxin
- 1S5F 2.6 Å, Cholera holotoxin, Crystal form 2
- 2A5G 2.66 Å, Cholera toxin A1 subunit bound to ARF6(Q67L)
Browse structure collections
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