2BYS: ACHBP FROM APLYSIA CALIFORNICA
CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA IN complex with lobeline. Determined by X-ray diffraction at 2.05 Å resolution. Released 5 Oct 2005.
- Method
- X-ray diffraction
- Resolution
- 2.05 Å
- Organism
- APLYSIA CALIFORNICA
- Chains
- 10
- Atoms
- 18,491
- Mol. weight
- 261.9 kDa
- Ligands
- LOB
- Released
- 5 Oct 2005
Explore 2BYS in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2BYS contains 36 α-helices and 150 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.
Chain A: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-14 | 12 | |
| β-strand | 29-44 | 16 | 1 |
| β-strand | 49-66 | 18 | 1 |
| α-helix | 69-71 | 3 | |
| β-strand | 77-81 | 5 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 2 |
| β-strand | 95 | 1 | 1 |
| β-strand | 100-101 | 2 | 1 |
| β-strand | 106-110 | 5 | 1 |
| β-strand | 112-117 | 6 | 1 |
| β-strand | 120-126 | 7 | 1 |
| β-strand | 138-146 | 9 | 2 |
| β-strand | 154-158 | 5 | 1 |
| β-strand | 162 | 1 | 2 |
| β-strand | 164 | 1 | 1 |
| β-strand | 174-187 | 14 | 2 |
| β-strand | 194-206 | 13 | 2 |
Chain B: 6 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-14 | 14 | |
| β-strand | 29-44 | 16 | 3 |
| β-strand | 49-61 | 13 | 3 |
| α-helix | 63-65 | 3 | |
| α-helix | 69-71 | 3 | |
| β-strand | 77-81 | 5 | 3 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 4 |
| β-strand | 95 | 1 | 3 |
| α-helix | 98-99 | 2 | |
| β-strand | 100-101 | 2 | 3 |
| β-strand | 106-110 | 5 | 3 |
| β-strand | 114-117 | 4 | 3 |
| β-strand | 120-126 | 7 | 3 |
| β-strand | 138-146 | 9 | 4 |
| β-strand | 154-157 | 4 | 3 |
| β-strand | 162 | 1 | 4 |
| α-helix | 163 | 1 | |
| β-strand | 164 | 1 | 3 |
| β-strand | 174-188 | 15 | 4 |
| β-strand | 191-206 | 16 | 4 |
Chains C and J: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-14 | 12 | |
| β-strand | 29-44 | 16 | 5 |
| β-strand | 49-66 | 18 | 5 |
| α-helix | 69-72 | 4 | |
| β-strand | 77-81 | 5 | 5 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 6 |
| β-strand | 95 | 1 | 5 |
| β-strand | 100-101 | 2 | 5 |
| β-strand | 106-110 | 5 | 5 |
| β-strand | 112-117 | 6 | 5 |
| β-strand | 120-126 | 7 | 5 |
| β-strand | 138-146 | 9 | 6 |
| β-strand | 154-157 | 4 | 5 |
| β-strand | 162 | 1 | 6 |
| β-strand | 164 | 1 | 5 |
| β-strand | 174-188 | 15 | 6 |
| β-strand | 191-206 | 16 | 6 |
Chain D: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-14 | 14 | |
| β-strand | 29-44 | 16 | 7 |
| β-strand | 49-66 | 18 | 7 |
| α-helix | 69-72 | 4 | |
| β-strand | 77-81 | 5 | 7 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 8 |
| β-strand | 95 | 1 | 7 |
| β-strand | 100-101 | 2 | 7 |
| β-strand | 106-110 | 5 | 7 |
| β-strand | 112-117 | 6 | 7 |
| β-strand | 120-126 | 7 | 7 |
| β-strand | 138-146 | 9 | 8 |
| β-strand | 154-157 | 4 | 7 |
| β-strand | 162 | 1 | 8 |
| β-strand | 164 | 1 | 7 |
| β-strand | 174-186 | 13 | 8 |
| β-strand | 195-206 | 12 | 8 |
Chain E: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-14 | 15 | |
| β-strand | 29-44 | 16 | 9 |
| β-strand | 49-66 | 18 | 9 |
| α-helix | 69-72 | 4 | |
| β-strand | 77-81 | 5 | 9 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 10 |
| β-strand | 95 | 1 | 9 |
| β-strand | 100-101 | 2 | 9 |
| β-strand | 106-110 | 5 | 9 |
| β-strand | 112-117 | 6 | 9 |
| β-strand | 120-126 | 7 | 9 |
| β-strand | 138-146 | 9 | 10 |
| β-strand | 154-157 | 4 | 9 |
| β-strand | 162 | 1 | 10 |
| β-strand | 164 | 1 | 9 |
| β-strand | 174-188 | 15 | 10 |
| β-strand | 191-206 | 16 | 10 |
Chain F: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-14 | 12 | |
| β-strand | 29-44 | 16 | 11 |
| β-strand | 49-66 | 18 | 11 |
| α-helix | 69-72 | 4 | |
| β-strand | 77-81 | 5 | 11 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 12 |
| β-strand | 95 | 1 | 11 |
| β-strand | 100-101 | 2 | 11 |
| β-strand | 106-110 | 5 | 11 |
| β-strand | 112-117 | 6 | 11 |
| β-strand | 120-126 | 7 | 11 |
| β-strand | 138-146 | 9 | 12 |
| β-strand | 154-157 | 4 | 11 |
| β-strand | 162 | 1 | 12 |
| β-strand | 164 | 1 | 11 |
| β-strand | 174-187 | 14 | 12 |
| β-strand | 194-206 | 13 | 12 |
Chain G: 5 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| β-strand | 29-44 | 16 | 13 |
| β-strand | 49-66 | 18 | 13 |
| α-helix | 69-71 | 3 | |
| β-strand | 77-81 | 5 | 13 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 14 |
| β-strand | 95 | 1 | 13 |
| α-helix | 98-99 | 2 | |
| β-strand | 100-101 | 2 | 13 |
| β-strand | 106-110 | 5 | 13 |
| β-strand | 112-117 | 6 | 13 |
| β-strand | 120-126 | 7 | 13 |
| β-strand | 138-146 | 9 | 14 |
| β-strand | 154-157 | 4 | 13 |
| β-strand | 162 | 1 | 14 |
| α-helix | 163 | 1 | |
| β-strand | 164 | 1 | 13 |
| β-strand | 174-188 | 15 | 14 |
| β-strand | 191-206 | 16 | 14 |
Chain H: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-14 | 13 | |
| β-strand | 29-44 | 16 | 15 |
| β-strand | 49-66 | 18 | 15 |
| α-helix | 69-72 | 4 | |
| β-strand | 77-81 | 5 | 15 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-92 | 3 | 16 |
| β-strand | 95 | 1 | 15 |
| β-strand | 100-101 | 2 | 15 |
| β-strand | 106-110 | 5 | 15 |
| β-strand | 112-117 | 6 | 15 |
| β-strand | 120-126 | 7 | 15 |
| β-strand | 138-146 | 9 | 16 |
| β-strand | 154-157 | 4 | 15 |
| β-strand | 162 | 1 | 16 |
| β-strand | 164 | 1 | 15 |
| β-strand | 174-188 | 15 | 16 |
| β-strand | 191-206 | 16 | 16 |
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 | 227 | APLYSIA CALIFORNICA | Q8WSF8 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA
>2BYS_1 ACETYLCHOLINE-BINDING PROTEIN (chains A, B, C, D, E, F, G, H, I, J)
YKDDDDKLHSQANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVKADSSTNEVDL
VYYEQQRWKLNSLMWDPNEYGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQIAVVTHD
GSVMFIPAQRLSFMCDPTGVDSEEGATCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASS
KYEILSATQTRQVQHYSCCPEPYIDVNLVVKFRERRAGNGFFRNLFD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| LOB | Lobeline | C22 H27 N O2 | 10 |
Primary citation
Structures of Aplysia Achbp Complexes with Nicotinic Agonists and Antagonists Reveal Distinctive Binding Interfaces and Conformations. Hansen, S.B., Sulzenbacher, G., Huxford, T. et al. EMBO J (2005) 24:3635. DOI 10.1038/SJ.EMBOJ.7600828 · PubMed
Other PDB entries of the same protein (UniProt Q8WSF8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6T9R 1.72 Å, Aplysia californica AChBP in complex with a cytisine derivative
- 2WN9 1.75 Å, Crystal structure of Aplysia ACHBP in complex with 4-0H-DMXBA
- 2PGZ 1.76 Å, Crystal structure of Cocaine bound to an ACh-Binding Protein
- 2WNJ 1.8 Å, Crystal structure of aplysia achbp in complex with dmxba
- 8QTL 1.85 Å, Aplysia californica acetylcholine-binding protein in complex with Spiroimine (-)-4 S
- 2Y7Y 1.9 Å, Aplysia californica achbp in apo state
- 4XHE 1.9 Å, Crystal Structure of A-AChBP in complex with pinnatoxin A
- 4ZK4 1.9 Å, Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica…
- 2XYS 1.91 Å, Crystal structure of Aplysia californica AChBP in complex with strychnine
- 5TVC 1.93 Å, Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica…
- 3C84 1.94 Å, Crystal structure of a complex of AChBP from aplysia californica and the neonicotinoid…
- 2YMD 1.96 Å, Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with serotonin…
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