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Three-dimensional structure of the membrane-embedded M2 channel-lining segment from the nicotinic acetylcholine receptor by solid-state NMR spectroscopy
Analyse Three-dimensional structure of the membrane-embedded M2 channel-lining segment… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CEK
- Type
- protein
- Length
- 15 residues
- Chains
- 1
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (acetylcholine receptor M2)
- UniProt
- P25110
Structure
solid-state nmr · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (acetylcholine receptor M2) | protein | 15 | 67% helix, 0% strand | P25110 |
Compared structures
- 1CEK · Three-dimensional structure of the membrane-embedded M2 channel-lining segment from the… · the same entry in another collection · chain A against A, TM-score 1.00
- P25110 · AlphaFold monomer V2.0 prediction for acetylcholine receptor subunit delta (P25110) · a predicted model of the same protein · chain A against A, TM-score 0.64
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 P25110
- Elsewhere: RCSB PDB 1CEK · PDBe 1CEK · UniProt P25110
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