Research workbench
Refined structure of the nicotinic acetylcholine receptor at 4A resolution.
Analyse Refined structure of the nicotinic acetylcholine receptor at 4A resolution. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BG9
- Type
- protein
- Length
- 1,849 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine receptor protein, alpha chain; Acetylcholine receptor protein, beta chain…
- UniProt
- P02711, Q6S3I0, Q6S3H8, Q6S3H9
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 4 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Acetylcholine receptor protein, alpha chain | protein | 370 | 42% helix, 23% strand | P02711 |
| B | Acetylcholine receptor protein, beta chain | protein | 370 | 38% helix, 19% strand | Q6S3I0 |
| C | Acetylcholine receptor protein, delta chain | protein | 369 | 42% helix, 22% strand | Q6S3H8 |
| E | Acetylcholine receptor protein, gamma chain | protein | 370 | 42% helix, 18% strand | Q6S3H9 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 633 | 0.87 | 0.91 | 89 | empty |
| 2 | 463 | 0.85 | 0.92 | 79 | empty |
| 3 | 437 | 0.83 | 0.90 | 46 | empty |
| 4 | 178 | 0.82 | 0.96 | 46 | empty |
| 5 | 468 | 0.79 | 0.86 | 64 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1948 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 1838 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 1739 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1518 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1395 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 2BG9 · Refined structure of the nicotinic acetylcholine receptor at 4A resolution. · the same entry in another collection · chain B against B, TM-score 1.00
- P02711 · AlphaFold monomer V2.0 prediction for acetylcholine receptor subunit alpha (P02711) · a predicted model of the same protein · chain D against A, TM-score 0.85
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 P02711
- Every structure of UniProt Q6S3I0
- Every structure of UniProt Q6S3H8
- Every structure of UniProt Q6S3H9
- Elsewhere: RCSB PDB 2BG9 · PDBe 2BG9 · UniProt P02711 · UniProt Q6S3I0 · UniProt Q6S3H8 · UniProt Q6S3H9
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