1UW6: Acetylcholine binding protein
X-ray structure of acetylcholine binding protein (AChBP) in complex with nicotine. Determined by X-ray diffraction at 2.2 Å resolution. Released 25 Mar 2004.
- Method
- X-ray diffraction
- Resolution
- 2.2 Å
- Organism
- LYMNAEA STAGNALIS
- Chains
- 20
- Atoms
- 34,788
- Mol. weight
- 483.76 kDa
- Ligands
- NCT
- Released
- 25 Mar 2004
Explore 1UW6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1UW6 contains 81 α-helices and 282 β-strands across 20 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: 4 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 27-42 | 16 | 1 |
| β-strand | 47-59 | 13 | 1 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 1 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 2 |
| β-strand | 91 | 1 | 1 |
| β-strand | 96-97 | 2 | 1 |
| β-strand | 102-106 | 5 | 1 |
| β-strand | 110-113 | 4 | 1 |
| β-strand | 116-122 | 7 | 1 |
| β-strand | 134-142 | 9 | 2 |
| β-strand | 150-154 | 5 | 1 |
| β-strand | 171-184 | 14 | 2 |
| β-strand | 191-203 | 13 | 2 |
| α-helix | 204-205 | 2 | |
Chain B: 3 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 27-42 | 16 | 3 |
| β-strand | 47-59 | 13 | 3 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 3 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 4 |
| β-strand | 91 | 1 | 3 |
| β-strand | 96-97 | 2 | 3 |
| β-strand | 102-106 | 5 | 3 |
| β-strand | 110-113 | 4 | 3 |
| β-strand | 116-122 | 7 | 3 |
| β-strand | 134-142 | 9 | 4 |
| β-strand | 150-154 | 5 | 3 |
| β-strand | 171-185 | 15 | 4 |
| β-strand | 188-203 | 16 | 4 |
Chains C and J: 4 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| β-strand | 22 | 1 | 5 |
| β-strand | 25 | 1 | 5 |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 6 |
| β-strand | 47-59 | 13 | 6 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 6 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 7 |
| β-strand | 91 | 1 | 6 |
| β-strand | 96-97 | 2 | 6 |
| β-strand | 102-106 | 5 | 6 |
| β-strand | 110-113 | 4 | 6 |
| β-strand | 116-122 | 7 | 6 |
| β-strand | 134-142 | 9 | 7 |
| β-strand | 150-154 | 5 | 6 |
| β-strand | 171-184 | 14 | 7 |
| β-strand | 191-203 | 13 | 7 |
Chain D: 4 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 8 |
| β-strand | 25 | 1 | 8 |
| β-strand | 27-42 | 16 | 9 |
| β-strand | 47-59 | 13 | 9 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 9 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 10 |
| β-strand | 91 | 1 | 9 |
| β-strand | 96-97 | 2 | 9 |
| β-strand | 102-106 | 5 | 9 |
| β-strand | 110-113 | 4 | 9 |
| β-strand | 116-122 | 7 | 9 |
| β-strand | 134-142 | 9 | 10 |
| β-strand | 150-153 | 4 | 9 |
| β-strand | 171-184 | 14 | 10 |
| β-strand | 191-203 | 13 | 10 |
| α-helix | 204-205 | 2 | |
Chains E and S: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 11 |
| β-strand | 25 | 1 | 11 |
| β-strand | 27-42 | 16 | 12 |
| β-strand | 47-59 | 13 | 12 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 12 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 13 |
| β-strand | 91 | 1 | 12 |
| β-strand | 96-97 | 2 | 12 |
| β-strand | 102-106 | 5 | 12 |
| β-strand | 110-113 | 4 | 12 |
| β-strand | 116-122 | 7 | 12 |
| β-strand | 134-142 | 9 | 13 |
| β-strand | 150-153 | 4 | 12 |
| β-strand | 171-184 | 14 | 13 |
| β-strand | 191-203 | 13 | 13 |
Chain F: 5 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| β-strand | 22 | 1 | 14 |
| β-strand | 25 | 1 | 14 |
| β-strand | 27-42 | 16 | 15 |
| β-strand | 47-59 | 13 | 15 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 15 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 16 |
| β-strand | 91 | 1 | 15 |
| β-strand | 96-97 | 2 | 15 |
| β-strand | 102-106 | 5 | 15 |
| β-strand | 110-113 | 4 | 15 |
| β-strand | 116-122 | 7 | 15 |
| β-strand | 134-142 | 9 | 16 |
| β-strand | 150-154 | 5 | 15 |
| α-helix | 161-164 | 4 | |
| β-strand | 171-184 | 14 | 16 |
| β-strand | 191-203 | 13 | 16 |
| α-helix | 204-205 | 2 | |
Chains G and K: 4 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 17 |
| β-strand | 25 | 1 | 17 |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 18 |
| β-strand | 47-59 | 13 | 18 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 18 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 19 |
| β-strand | 91 | 1 | 18 |
| β-strand | 96-97 | 2 | 18 |
| β-strand | 102-106 | 5 | 18 |
| β-strand | 110-113 | 4 | 18 |
| β-strand | 116-122 | 7 | 18 |
| β-strand | 134-142 | 9 | 19 |
| β-strand | 150-154 | 5 | 18 |
| β-strand | 171-184 | 14 | 19 |
| β-strand | 191-203 | 13 | 19 |
Chain H: 4 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 20 |
| β-strand | 47-59 | 13 | 20 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 20 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 21 |
| β-strand | 91 | 1 | 20 |
| β-strand | 96-97 | 2 | 20 |
| β-strand | 102-106 | 5 | 20 |
| β-strand | 110-113 | 4 | 20 |
| β-strand | 116-122 | 7 | 20 |
| β-strand | 134-142 | 9 | 21 |
| β-strand | 150-154 | 5 | 20 |
| β-strand | 171-184 | 14 | 21 |
| β-strand | 191-203 | 13 | 21 |
8 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Acetylcholine-binding protein | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T | protein | 211 | LYMNAEA STAGNALIS | P58154 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T), FASTA
>1UW6_1 ACETYLCHOLINE-BINDING PROTEIN (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T)
EFDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWS
DRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQ
RFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQK
KNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NCT | (s)-3-(1-methylpyrrolidin-2-yl)pyridine | C10 H14 N2 | 20 |
Primary citation
Nicotine and Carbamylcholine Binding to Nicotinic Acetylcholine Receptors as Studied in Achbp Crystal Structures. Celie, P.H.N., Van Rossum-Fikkert, S.E., Van Dijk, W.J. et al. Neuron (2004) 41:907. DOI 10.1016/S0896-6273(04)00115-1 · PubMed
Other PDB entries of the same protein (UniProt P58154 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7NDV 1.7 Å, X-ray structure of acetylcholine-binding protein (AChBP) in complex with FL001888.
- 4ZK1 1.75 Å, Crystal Structure of Lymnaea stagnalis Acetylcholine-Binding Protein (LsAChBP) in…
- 4ZJT 1.85 Å, X-ray crystal structure of Lymnaea stagnalis acetylcholine binding protein (LsAChBP) in…
- 4ZRU 1.9 Å, X-ray crystal structure of Lymnaea stagnalis acetylcholine binding protein (Ls-AChBP) in…
- 8P11 1.9 Å, X-ray structure of acetylcholine-binding protein (AChBP) in complex with FL003044.
- 7NDP 2.0 Å, X-ray structure of acetylcholine-binding protein (AChBP) in complex with FL001856.
- 7PD6 2.0 Å, Crystal structure of Lymnaea stagnalis Acetylcholine-binding protein (Ls-AChBP)…
- 7PE6 2.01 Å, Crystal structure of Lymnaea stagnalis Acetylcholine-binding protein (Ls-AChBP)…
- 5J5G 2.04 Å, X-Ray Crystal Structure of Acetylcholine Binding Protein (AChBP) in Complex with…
- 5J5F 2.04 Å, X-Ray Crystal Structure of Acetylcholine Binding Protein (AChBP) in Complex with…
- 3WTN 2.09 Å, Crystal Structure of Lymnaea stagnalis Acetylcholine Binding Protein Complexed with…
- 4QAC 2.1 Å, X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP) IN COMPLEX WITH…
Browse structure collections
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