Research workbench
Crystal structure of the extracellular domain of the human ALPHA9 nicotinic acetylcholine receptor
Analyse Crystal structure of the extracellular domain of the human ALPHA9 nicotinic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D01
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neuronal acetylcholine receptor subunit alpha-9
- UniProt
- Q9UGM1
- Ligands
- NAG
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neuronal acetylcholine receptor subunit alpha-9 | protein | 212 | 8% helix, 52% strand | Q9UGM1 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.48 | 0.75 | 26 | empty |
Modifications
Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 4D01 · Crystal Structure of the Extracellular Domain of the Human Alpha9 Nicotinic Acetylcholine… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UGM1 · AlphaFold monomer V2.0 prediction for neuronal acetylcholine receptor subunit alpha-9… · a predicted model of the same protein · chain A against A, TM-score 0.93
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9UGM1
- Elsewhere: RCSB PDB 4D01 · PDBe 4D01 · UniProt Q9UGM1
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