MolNFT v1 · #88606 · protein
Crystal structure of the extracellular domain of the human ALPHA9 nicotinic acetylcholine receptor
4D01 · Neuronal acetylcholine receptor subunit alpha-9: “Crystal structure of the extracellular domain of the human ALPHA9 nicotinic acetylcholine receptor”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.48). MolNFT v1…
- 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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