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

ElementResiduesLengthSheet
α-helix3-1311
β-strand2211
β-strand2511
α-helix261
β-strand27-42162
β-strand47-59132
α-helix61-633
β-strand73-7752
α-helix78-803
β-strand86-8833
β-strand9112
β-strand96-9722
β-strand102-10652
β-strand110-11342
β-strand116-12272
β-strand134-14293
β-strand150-15452
β-strand171-184143
β-strand191-203133
Chain B: 3 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix3-1210
β-strand2214
β-strand2514
β-strand27-42165
β-strand47-59135
α-helix61-633
β-strand73-7755
α-helix78-803
β-strand86-8836
β-strand9115
β-strand96-9725
β-strand102-10655
β-strand110-11345
β-strand116-12275
β-strand134-14296
β-strand150-15345
β-strand171-184146
β-strand191-203136
Chain C: 4 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix3-1210
α-helix261
β-strand27-42167
β-strand47-59137
α-helix61-633
β-strand73-7757
α-helix78-803
β-strand86-8838
β-strand9117
β-strand96-9727
β-strand102-10657
β-strand110-11347
β-strand116-12277
β-strand134-14298
β-strand150-15457
β-strand171-184148
β-strand191-203138
Chain D: 4 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix3-1311
β-strand2219
β-strand2519
α-helix261
β-strand27-381210
β-strand42110
β-strand47-591310
α-helix61-633
β-strand73-77510
α-helix78-803
β-strand86-88311
β-strand91110
β-strand96-97210
β-strand102-106510
β-strand110-113410
β-strand116-122710
β-strand134-142911
β-strand150-154510
β-strand171-1831311
β-strand192-2031211
Chain E: 3 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix3-1210
α-helix261
β-strand27-421612
β-strand47-591312
β-strand73-77512
α-helix78-803
β-strand86-88313
β-strand91112
β-strand96-97212
β-strand102-106512
β-strand110-113412
β-strand116-122712
β-strand134-142913
β-strand150-154512
β-strand171-177713
β-strand180-184513
β-strand191-2031313
Chain F: 3 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix3-1311
β-strand22114
β-strand25114
α-helix261
β-strand27-421615
β-strand47-591315
β-strand73-77515
α-helix78-803
β-strand86-88316
β-strand91115
β-strand96-97215
β-strand102-106515
β-strand110-113415
β-strand116-122715
β-strand134-142916
β-strand150-154515
β-strand171-1841416
β-strand191-2031316
Chain G: 4 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix3-1210
β-strand22117
β-strand25117
α-helix261
β-strand27-421618
β-strand47-591318
α-helix61-633
β-strand73-77518
α-helix78-803
β-strand86-88319
β-strand91118
β-strand96-97218
β-strand102-106518
β-strand110-113418
β-strand116-122718
β-strand134-142919
β-strand150-154518
β-strand171-1841419
β-strand191-2031319
Chain I: 4 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix3-1311
β-strand22123
β-strand25123
α-helix261
β-strand27-381224
β-strand42124
β-strand47-591324
α-helix61-633
β-strand73-77524
α-helix78-803
β-strand86-88325
β-strand91124
β-strand96-97224
β-strand102-106524
β-strand110-113424
β-strand116-122724
β-strand134-142925
β-strand150-154524
β-strand171-1841425
β-strand191-2031325

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Acetylcholine-binding proteinA, B, C, D, E, F, G, H, I, Jprotein214Lymnaea stagnalisP58154 (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

IDNameFormulaCopies
N2Y(2Z)-1-[(6-chloropyridin-3-yl)methyl]imidazolidin-2-imineC9 H11 Cl N410
CDCadmium ionCd54

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:

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