Research workbench
Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class)
Analyse Gating movement in acetylcholine receptor analysed by time- resolved electron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AQ9
- Type
- protein
- Length
- 1,849 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine receptor subunit alpha; Acetylcholine receptor beta subunit; Acetylcholine…
- UniProt
- P02711, Q6S3I0, Q6S3H8, Q6S3H9
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 4 distinct chains · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Acetylcholine receptor subunit alpha | protein | 370 | 41% helix, 21% strand | P02711 |
| B | Acetylcholine receptor beta subunit | protein | 370 | 36% helix, 18% strand | Q6S3I0 |
| C | Acetylcholine receptor delta subunit | protein | 369 | 38% helix, 22% strand | Q6S3H8 |
| E | Acetylcholine receptor gamma subunit | protein | 370 | 39% 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 | 1004 | 0.87 | 0.88 | 139 | empty |
| 2 | 643 | 0.87 | 0.91 | 83 | empty |
| 3 | 396 | 0.86 | 0.94 | 65 | empty |
| 4 | 840 | 0.85 | 0.87 | 87 | empty |
| 5 | 334 | 0.83 | 0.92 | 67 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1945 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 1809 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1649 Ų buried · 3 hydrogen bonds · protein-protein
- A–E · 1612 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1569 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 4AQ9 · Gating movement in acetylcholine receptor analysed by time- resolved electron… · 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 A 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 4AQ9 · PDBe 4AQ9 · UniProt P02711 · UniProt Q6S3I0 · UniProt Q6S3H8 · UniProt Q6S3H9
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