5AFH: Alpha7-AChBP
alpha7-AChBP in complex with lobeline. Determined by X-ray diffraction at 2.4 Å resolution. Released 6 May 2015.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organisms
- HOMO SAPIENS, LYMNAEA STAGNALIS
- Chains
- 5
- Atoms
- 9,032
- Mol. weight
- 122.62 kDa
- Ligands
- L0B
- Released
- 6 May 2015
Explore 5AFH in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5AFH contains 23 α-helices and 76 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.
Chain A: 4 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-11 | 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 | 75-79 | 5 | 2 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 3 |
| β-strand | 93 | 1 | 2 |
| β-strand | 98-99 | 2 | 2 |
| β-strand | 104-108 | 5 | 2 |
| β-strand | 112-115 | 4 | 2 |
| β-strand | 118-124 | 7 | 2 |
| β-strand | 136-144 | 9 | 3 |
| β-strand | 152-156 | 5 | 2 |
| β-strand | 160 | 1 | 2 |
| β-strand | 170-182 | 13 | 3 |
| β-strand | 191-202 | 12 | 3 |
Chain B: 5 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-11 | 10 | |
| β-strand | 22 | 1 | 4 |
| β-strand | 25 | 1 | 4 |
| α-helix | 26 | 1 | |
| β-strand | 27-42 | 16 | 5 |
| β-strand | 47-59 | 13 | 5 |
| α-helix | 61-63 | 3 | |
| β-strand | 75-79 | 5 | 5 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 6 |
| β-strand | 93 | 1 | 5 |
| β-strand | 98-99 | 2 | 5 |
| β-strand | 104-108 | 5 | 5 |
| β-strand | 112-115 | 4 | 5 |
| β-strand | 118-124 | 7 | 5 |
| α-helix | 128-131 | 4 | |
| β-strand | 136-144 | 9 | 6 |
| β-strand | 152-156 | 5 | 5 |
| β-strand | 170-182 | 13 | 6 |
| β-strand | 191-202 | 12 | 6 |
Chain C: 5 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-10 | 10 | |
| β-strand | 22-23 | 2 | 7 |
| β-strand | 25 | 1 | 7 |
| α-helix | 26 | 1 | |
| β-strand | 27-38 | 12 | 8 |
| β-strand | 50-59 | 10 | 8 |
| α-helix | 61-63 | 3 | |
| β-strand | 75-79 | 5 | 8 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 9 |
| β-strand | 93 | 1 | 10 |
| β-strand | 98-99 | 2 | 8 |
| β-strand | 104-108 | 5 | 8 |
| β-strand | 112-115 | 4 | 8 |
| β-strand | 118-121 | 4 | 8 |
| β-strand | 123 | 1 | 10 |
| β-strand | 136-144 | 9 | 9 |
| β-strand | 152-156 | 5 | 8 |
| α-helix | 157-159 | 3 | |
| β-strand | 170-182 | 13 | 9 |
| β-strand | 191-202 | 12 | 9 |
Chain D: 4 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-11 | 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 | |
| α-helix | 67-69 | 3 | |
| β-strand | 75-79 | 5 | 12 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 13 |
| β-strand | 93 | 1 | 12 |
| β-strand | 98-99 | 2 | 12 |
| β-strand | 104-108 | 5 | 12 |
| β-strand | 112-115 | 4 | 12 |
| β-strand | 118-124 | 7 | 12 |
| β-strand | 136-144 | 9 | 13 |
| β-strand | 152-156 | 5 | 12 |
| β-strand | 160 | 1 | 12 |
| β-strand | 170-182 | 13 | 13 |
| β-strand | 191-202 | 12 | 13 |
Chain E: 5 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-11 | 11 | |
| α-helix | 25-26 | 2 | |
| β-strand | 27-42 | 16 | 14 |
| β-strand | 47-64 | 18 | 14 |
| α-helix | 67-69 | 3 | |
| β-strand | 75-79 | 5 | 14 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 15 |
| β-strand | 93 | 1 | 14 |
| β-strand | 98-99 | 2 | 14 |
| β-strand | 104-108 | 5 | 14 |
| β-strand | 110-115 | 6 | 14 |
| β-strand | 118-124 | 7 | 14 |
| α-helix | 128-130 | 3 | |
| β-strand | 136-144 | 9 | 15 |
| β-strand | 152-156 | 5 | 14 |
| β-strand | 170-182 | 13 | 15 |
| β-strand | 191-202 | 12 | 15 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Acetylcholine-binding protein, neuronal acetylcholine receptor subunit alpha-7 | A, B, C, D, E | protein | 205 | HOMO SAPIENS, LYMNAEA STAGNALIS | P36544 (AlphaFold model), P58154 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>5AFH_1 ACETYLCHOLINE-BINDING PROTEIN, NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-7 (chains A, B, C, D, E)
GEFQRKLYKELVKNYNPDVIPTQRDRPVTVYFSLSLLQIMDVDEKNQVVDVVFWLQMSWT
DHYLQWNVSEYPGVKQVSVPISSLWVPDLAAYNAISKPEVLTPQLALVNSSGHVQYLPSI
RQRFSCDVSGVDTESGATCKLKFGSWTHHSRELDLQMQEADISGYIPYSRFELVGVTQKR
SERFYECCKEPYPDVTFTVTFRKKG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| L0B | Alpha-Lobeline | C22 H27 N O2 | 5 |
Primary citation
Molecular Blueprint of Allosteric Binding Sites in a Homologue of the Agonist-Binding Domain of the Alpha7 Nicotinic Acetylcholine Receptor. Spurny, R., Debaveye, S., Farinha, A. et al. Proc Natl Acad Sci U S A (2015) 112:E2543. DOI 10.1073/PNAS.1418289112 · PubMed
Other PDB entries of the same protein (UniProt P36544 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8P1H 1.95 Å, Crystal structure of the chimera of human 14-3-3 zeta and phosphorylated cytoplasmic…
- 5AFN 2.15 Å, alpha7-AChBP in complex with lobeline and fragment 5
- 9QTO 2.16 Å, Human alpha7 nicotinic receptor in complex with the E6 nanobody
- 8V8A 2.19 Å, Alpha7-nicotinic acetylcholine receptor time resolved bound to epibatidine and…
- 5AFJ 2.2 Å, alpha7-AChBP in complex with lobeline and fragment 1
- 9QTN 2.28 Å, Human alpha7 nicotinic receptor in complex with the F1 nanobody
- 8C9X 2.3 Å, human alpha7 nicotinic receptor in complex with the C4 nanobody
- 8UT1 2.3 Å, Alpha7-nicotinic acetylcholine receptor bound to epibatidine
- 8UTB 2.3 Å, Alpha7-nicotinic acetylcholine receptor bound to epibatidine and NS-1738
- 8UZJ 2.3 Å, Alpha7-nicotinic acetylcholine receptor bound to epibatidine and ivermectin
- 8V88 2.3 Å, Alpha7-nicotinic acetylcholine receptor bound to epibatidine and GAT107
- 8V80 2.34 Å, Alpha7-nicotinic acetylcholine receptor bound to epibatidine and (-)-TQS
Browse structure collections
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