Research workbench
AlphaFold monomer V2.0 prediction for glycine receptor subunit alpha-1 (P23415)
Analyse AlphaFold monomer V2.0 prediction for glycine receptor subunit alpha-1 (P23415) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23415
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- UniProt
- P23415
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 457 | — | P23415 |
Compared structures
- 8DN2 · Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state… · an experimental structure of the same protein · chain A against D, TM-score 0.74
- 8DN5 · Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound… · an experimental structure of the same protein · chain A against A, TM-score 0.74
- 8DN4 · Cryo-EM structure of human Glycine Receptor alpha-1 beta heteromer, glycine-bound… · an experimental structure of the same protein · chain A against D, TM-score 0.73
- 8DN3 · Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, apo state · an experimental structure of the same protein · chain A against C, TM-score 0.71
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 P23415
- Elsewhere: UniProt P23415 · AlphaFold DB P23415
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