Cholera toxin B-pentamer complexed with GM1 pentasaccharide. Determined by X-ray diffraction at 2.0 Å resolution. Released 3 Dec 1997.
Explore 2CHB in 3D Show helices and sheets RCSB PDB PDBe
2CHB contains 20 α-helices and 30 β-strands across 5 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 | 5-9 | 5 | |
| β-strand | 15-23 | 9 | 1 |
| β-strand | 26-30 | 5 | 1 |
| β-strand | 38-41 | 4 | 1 |
| β-strand | 47-50 | 4 | 1 |
| α-helix | 51-53 | 3 | |
| α-helix | 61-78 | 18 | |
| α-helix | 80 | 1 | |
| β-strand | 81-88 | 8 | 1 |
| β-strand | 94-102 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-23 | 9 | 1 |
| β-strand | 26-30 | 5 | 1 |
| β-strand | 38-41 | 4 | 1 |
| β-strand | 47-50 | 4 | 1 |
| α-helix | 51-53 | 3 | |
| α-helix | 59-61 | 3 | |
| α-helix | 62-78 | 17 | |
| α-helix | 80 | 1 | |
| β-strand | 81-88 | 8 | 1 |
| β-strand | 94-102 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-23 | 9 | 1 |
| β-strand | 26-30 | 5 | 1 |
| β-strand | 38-41 | 4 | 1 |
| β-strand | 47-50 | 4 | 1 |
| α-helix | 60-77 | 18 | |
| α-helix | 80 | 1 | |
| β-strand | 81-88 | 8 | 1 |
| β-strand | 94-102 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-23 | 9 | 1 |
| β-strand | 26-30 | 5 | 1 |
| β-strand | 38-41 | 4 | 1 |
| β-strand | 47-50 | 4 | 1 |
| α-helix | 51-53 | 3 | |
| α-helix | 59-78 | 20 | |
| α-helix | 80 | 1 | |
| β-strand | 81-88 | 8 | 1 |
| β-strand | 94-102 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-9 | 5 | |
| β-strand | 15-23 | 9 | 1 |
| β-strand | 26-30 | 5 | 1 |
| β-strand | 38-41 | 4 | 1 |
| β-strand | 47-50 | 4 | 1 |
| α-helix | 51-53 | 3 | |
| α-helix | 61-77 | 17 | |
| α-helix | 80 | 1 | |
| β-strand | 81-88 | 8 | 1 |
| β-strand | 94-102 | 9 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cholera toxin | D, E, F, G, H | protein | 104 | Vibrio cholerae | P01556 (AlphaFold model) |
>2CHB_1 CHOLERA TOXIN (chains D, E, F, G, H) MTPQNITDLCAEYHNTQIHTLNDKIFSYTESLAGKREMAIITFKNGATFQVEVPGSQHID SQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN
Structural studies of receptor binding by cholera toxin mutants. Merritt, E.A., Sarfaty, S., Jobling, M.G. et al. Protein Sci (1997) 6:1516-1528. PubMed
Other PDB entries of the same protein (UniProt P01556 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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