MolNFT v1 · #85894 · protein
Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class)
4AQ9: “Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class)”. Electron microscopy. MolNFT v1 #85894 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4AQ9
- Type
- protein
- Length
- 1,849 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02711, Q6S3I0, Q6S3H8, Q6S3H9
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 370 | — | P02711 |
| B | — | protein | 370 | — | Q6S3I0 |
| C | — | protein | 369 | — | Q6S3H8 |
| E | — | protein | 370 | — | Q6S3H9 |
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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