3WTN: Lymnaea stagnalis Acetylcholine Binding Protein
Crystal Structure of Lymnaea stagnalis Acetylcholine Binding Protein Complexed with Desnitro-imidacloprid. Determined by X-ray diffraction at 2.09 Å resolution. Released 4 Feb 2015.
- Method
- X-ray diffraction
- Resolution
- 2.09 Å
- Organism
- Lymnaea stagnalis
- Chains
- 10
- Atoms
- 18,230
- Mol. weight
- 250.44 kDa
- Ligands
- N2Y, CD
- Released
- 4 Feb 2015
Explore 3WTN in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3WTN contains 37 α-helices and 149 β-strands across 10 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.
Chains A and H: 4 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 1 |
| β-strand | 25 | 1 | 1 |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 2 |
| β-strand | 47-59 | 13 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 2 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 3 |
| β-strand | 91 | 1 | 2 |
| β-strand | 96-97 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 110-113 | 4 | 2 |
| β-strand | 116-122 | 7 | 2 |
| β-strand | 134-142 | 9 | 3 |
| β-strand | 150-154 | 5 | 2 |
| β-strand | 171-184 | 14 | 3 |
| β-strand | 191-203 | 13 | 3 |
Chain B: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| β-strand | 22 | 1 | 4 |
| β-strand | 25 | 1 | 4 |
| β-strand | 27-42 | 16 | 5 |
| β-strand | 47-59 | 13 | 5 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 5 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 6 |
| β-strand | 91 | 1 | 5 |
| β-strand | 96-97 | 2 | 5 |
| β-strand | 102-106 | 5 | 5 |
| β-strand | 110-113 | 4 | 5 |
| β-strand | 116-122 | 7 | 5 |
| β-strand | 134-142 | 9 | 6 |
| β-strand | 150-153 | 4 | 5 |
| β-strand | 171-184 | 14 | 6 |
| β-strand | 191-203 | 13 | 6 |
Chain C: 4 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 7 |
| β-strand | 47-59 | 13 | 7 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 7 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 8 |
| β-strand | 91 | 1 | 7 |
| β-strand | 96-97 | 2 | 7 |
| β-strand | 102-106 | 5 | 7 |
| β-strand | 110-113 | 4 | 7 |
| β-strand | 116-122 | 7 | 7 |
| β-strand | 134-142 | 9 | 8 |
| β-strand | 150-154 | 5 | 7 |
| β-strand | 171-184 | 14 | 8 |
| β-strand | 191-203 | 13 | 8 |
Chain D: 4 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 9 |
| β-strand | 25 | 1 | 9 |
| α-helix | 26 | 1 | |
| β-strand | 27-38 | 12 | 10 |
| β-strand | 42 | 1 | 10 |
| β-strand | 47-59 | 13 | 10 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 10 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 11 |
| β-strand | 91 | 1 | 10 |
| β-strand | 96-97 | 2 | 10 |
| β-strand | 102-106 | 5 | 10 |
| β-strand | 110-113 | 4 | 10 |
| β-strand | 116-122 | 7 | 10 |
| β-strand | 134-142 | 9 | 11 |
| β-strand | 150-154 | 5 | 10 |
| β-strand | 171-183 | 13 | 11 |
| β-strand | 192-203 | 12 | 11 |
Chain E: 3 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 12 |
| β-strand | 47-59 | 13 | 12 |
| 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 | 150-154 | 5 | 12 |
| β-strand | 171-177 | 7 | 13 |
| β-strand | 180-184 | 5 | 13 |
| β-strand | 191-203 | 13 | 13 |
Chain F: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 14 |
| β-strand | 25 | 1 | 14 |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 15 |
| β-strand | 47-59 | 13 | 15 |
| 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 |
| β-strand | 171-184 | 14 | 16 |
| β-strand | 191-203 | 13 | 16 |
Chain G: 4 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| 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 I: 4 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| β-strand | 22 | 1 | 23 |
| β-strand | 25 | 1 | 23 |
| α-helix | 26 | 1 | |
| β-strand | 27-38 | 12 | 24 |
| β-strand | 42 | 1 | 24 |
| β-strand | 47-59 | 13 | 24 |
| α-helix | 61-63 | 3 | |
| β-strand | 73-77 | 5 | 24 |
| α-helix | 78-80 | 3 | |
| β-strand | 86-88 | 3 | 25 |
| β-strand | 91 | 1 | 24 |
| β-strand | 96-97 | 2 | 24 |
| β-strand | 102-106 | 5 | 24 |
| β-strand | 110-113 | 4 | 24 |
| β-strand | 116-122 | 7 | 24 |
| β-strand | 134-142 | 9 | 25 |
| β-strand | 150-154 | 5 | 24 |
| β-strand | 171-184 | 14 | 25 |
| β-strand | 191-203 | 13 | 25 |
1 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 | protein | 214 | Lymnaea stagnalis | P58154 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA
>3WTN_1 Acetylcholine-binding protein (chains A, B, C, D, E, F, G, H, I, J)
EAEAADRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQT
TWSDRTLAWDSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPS
IRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDV
TQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| N2Y | (2Z)-1-[(6-chloropyridin-3-yl)methyl]imidazolidin-2-imine | C9 H11 Cl N4 | 10 |
| CD | Cadmium ion | Cd | 54 |
Water and common crystallization additives (NA) are not listed.
Primary citation
Studies on an acetylcholine binding protein identify a basic residue in loop G on the beta 1 strand as a new structural determinant of neonicotinoid actions. Ihara, M., Okajima, T., Yamashita, A. et al. Mol Pharmacol (2014) 86:736-746. DOI 10.1124/mol.114.094698 · 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…
- 4QAC 2.1 Å, X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP) IN COMPLEX WITH…
- 7PE5 2.1 Å, Crystal structure of Lymnaea stagnalis Acetylcholine-binding protein (Ls-AChBP)…
Browse structure collections
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