Crystal structure of alpha9 nAChR extracellular domain in complex with alpha-conotoxin RgIA. Determined by X-ray diffraction at 2.26 Å resolution. Released 22 May 2019.
Explore 6HY7 in 3D Show helices and sheets RCSB PDB PDBe
6HY7 contains 8 α-helices and 17 β-strands across 2 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 | 3-14 | 12 | |
| β-strand | 31-46 | 16 | 1 |
| β-strand | 51-68 | 18 | 1 |
| α-helix | 71-73 | 3 | |
| β-strand | 79-83 | 5 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 92-94 | 3 | 2 |
| β-strand | 97 | 1 | 1 |
| β-strand | 109-113 | 5 | 1 |
| β-strand | 115-129 | 15 | 1 |
| β-strand | 130-133 | 4 | 2 |
| β-strand | 141-150 | 10 | 2 |
| β-strand | 158-162 | 5 | 1 |
| β-strand | 166 | 1 | 3 |
| β-strand | 168 | 1 | 1 |
| α-helix | 172 | 1 | |
| β-strand | 173 | 1 | 1 |
| α-helix | 174-175 | 2 | |
| β-strand | 178-182 | 5 | 2 |
| β-strand | 184 | 1 | 3 |
| β-strand | 185-190 | 6 | 2 |
| α-helix | 196-198 | 3 | |
| β-strand | 199-210 | 12 | 2 |
| α-helix | 211-212 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neuronal acetylcholine receptor subunit alpha-9 | A | protein | 218 | Homo sapiens | Q9UGM1 (AlphaFold model) |
| Alpha-conotoxin RgIA | B | protein | 13 | Conus regius | P0C1D0 (AlphaFold model) |
>6HY7_1 Neuronal acetylcholine receptor subunit alpha-9 (chains A) ADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQ IWHDAYLTWDRDQYDGLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITW DAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEV HGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSHHHHHH
>6HY7_2 Alpha-conotoxin RgIA (chains B) GCCSDPRCRYRCR
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (EDO) are not listed.
Crystal Structure of the Monomeric Extracellular Domain of alpha 9 Nicotinic Receptor Subunit in Complex With alpha-Conotoxin RgIA: Molecular Dynamics Insights Into RgIA Binding to alpha 9 alpha 10 Nicotinic Receptors. Zouridakis, M., Papakyriakou, A., Ivanov, I.A. et al. Front Pharmacol (2019) 10:474-474. DOI 10.3389/fphar.2019.00474 · PubMed
Other PDB entries of the same protein (UniProt Q9UGM1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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