Aplysia californica achbp in apo state. Determined by X-ray diffraction at 1.9 Å resolution. Released 23 Mar 2011.
Explore 2Y7Y in 3D Show helices and sheets RCSB PDB PDBe
2Y7Y contains 24 α-helices and 79 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 | 2-12 | 11 | |
| β-strand | 27-42 | 16 | 1 |
| β-strand | 47-64 | 18 | 1 |
| α-helix | 67-69 | 3 | |
| β-strand | 75-79 | 5 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 2 |
| β-strand | 93 | 1 | 1 |
| β-strand | 98-99 | 2 | 1 |
| β-strand | 104-108 | 5 | 1 |
| β-strand | 110-115 | 6 | 1 |
| β-strand | 118-124 | 7 | 1 |
| β-strand | 136-144 | 9 | 2 |
| β-strand | 152-155 | 4 | 1 |
| β-strand | 160 | 1 | 2 |
| β-strand | 162 | 1 | 1 |
| β-strand | 172-184 | 13 | 2 |
| β-strand | 193-204 | 12 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-8 | 7 | |
| α-helix | 9-13 | 5 | |
| α-helix | 16-18 | 3 | |
| β-strand | 27-42 | 16 | 3 |
| β-strand | 47-64 | 18 | 3 |
| α-helix | 67-69 | 3 | |
| β-strand | 75-79 | 5 | 3 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 4 |
| β-strand | 93 | 1 | 3 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-99 | 2 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 110-115 | 6 | 3 |
| β-strand | 118-124 | 7 | 3 |
| β-strand | 136-144 | 9 | 4 |
| β-strand | 152-155 | 4 | 3 |
| β-strand | 160 | 1 | 4 |
| β-strand | 162 | 1 | 3 |
| β-strand | 172-184 | 13 | 4 |
| β-strand | 193-204 | 12 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-12 | 11 | |
| β-strand | 27-42 | 16 | 5 |
| β-strand | 47-64 | 18 | 5 |
| α-helix | 67-70 | 4 | |
| β-strand | 75-79 | 5 | 5 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 6 |
| β-strand | 93 | 1 | 5 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-99 | 2 | 5 |
| β-strand | 104-108 | 5 | 5 |
| β-strand | 110-115 | 6 | 5 |
| β-strand | 118-124 | 7 | 5 |
| β-strand | 136-144 | 9 | 6 |
| β-strand | 152-155 | 4 | 5 |
| β-strand | 160 | 1 | 6 |
| β-strand | 162 | 1 | 5 |
| β-strand | 172-183 | 12 | 6 |
| β-strand | 194-204 | 11 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-12 | 11 | |
| α-helix | 16-18 | 3 | |
| β-strand | 22 | 1 | 7 |
| β-strand | 25 | 1 | 7 |
| β-strand | 27-42 | 16 | 8 |
| β-strand | 47-64 | 18 | 8 |
| α-helix | 67-70 | 4 | |
| β-strand | 75-79 | 5 | 8 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 9 |
| β-strand | 93 | 1 | 8 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-99 | 2 | 8 |
| β-strand | 104-108 | 5 | 8 |
| β-strand | 110-115 | 6 | 8 |
| β-strand | 118-124 | 7 | 8 |
| β-strand | 136-144 | 9 | 9 |
| β-strand | 152-155 | 4 | 8 |
| β-strand | 160 | 1 | 9 |
| α-helix | 161 | 1 | |
| β-strand | 162 | 1 | 8 |
| β-strand | 172-184 | 13 | 9 |
| β-strand | 193-204 | 12 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-12 | 11 | |
| α-helix | 16-18 | 3 | |
| β-strand | 22 | 1 | 10 |
| β-strand | 25 | 1 | 10 |
| β-strand | 27-42 | 16 | 11 |
| β-strand | 47-64 | 18 | 11 |
| α-helix | 67-70 | 4 | |
| β-strand | 75-79 | 5 | 11 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 12 |
| β-strand | 93 | 1 | 11 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-99 | 2 | 11 |
| β-strand | 104-108 | 5 | 11 |
| β-strand | 110-115 | 6 | 11 |
| β-strand | 118-124 | 7 | 11 |
| β-strand | 136-144 | 9 | 12 |
| β-strand | 152-155 | 4 | 11 |
| β-strand | 160 | 1 | 12 |
| β-strand | 162 | 1 | 11 |
| β-strand | 172-184 | 13 | 12 |
| β-strand | 193-204 | 12 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Soluble acetylcholine receptor | A, B, C, D, E | protein | 217 | APLYSIA CALIFORNICA | Q8WSF8 (AlphaFold model) |
>2Y7Y_1 SOLUBLE ACETYLCHOLINE RECEPTOR (chains A, B, C, D, E) QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVKVDSSTNEVDLVYYEQQRWKL NSLMWDPNEYGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQT RQVQHYSCCPEPYIDVNLVVKFRERRAGNGFFRNLFD
Use of Acetylcholine Binding Protein in the Search for Novel Alpha7 Nicotinic Receptor Ligands. In Silico Docking, Pharmacological Screening, and X-Ray Analysis. Ulens, C., Akdemir, A., Jongejan, A. et al. J Med Chem (2009) 52:2372. DOI 10.1021/JM801400G · PubMed
Other PDB entries of the same protein (UniProt Q8WSF8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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