Neuronal acetylcholine receptor subunit alpha-7 (CHRNA7) is a 502-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P36544.
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The mean pLDDT of this model is 78.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 38% |
| 70 to 90 | Confident: backbone generally right | 38% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Component of neuronal acetylcholine receptors (nAChRs) that function as pentameric, ligand-gated cation channels with high calcium permeability among other activities. nAChRs are excitatory neurotrasnmitter receptors formed by a collection of nAChR subunits known to mediate synaptic transmission in the nervous system and the neuromuscular junction. Each nAchR subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, cation permeability, and binding to allosteric modulators (PubMed:15609996, PubMed:33735609, PubMed:8145738). CHRNA7 forms homopentameric neuronal acetylcholine receptors abundantly expressed…
Homopentamer (PubMed:33735609, PubMed:38382524). Can also form heteropentamers with CHRNB2, mainly found in basal forebrain cholinergic neurons (PubMed:33239400, PubMed:38161283). Interacts with RIC3; which is required for proper folding and assembly (PubMed:15504725, PubMed:16120769). Interacts with LYPD6 (PubMed:27344019). Interacts with CANX (PubMed:32783947)
Postsynaptic cell membrane, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8P1H | X-ray | 1.95 Å | A/B=361-372 |
| 5AFN | X-ray | 2.15 Å | A/B/C/D/E=23-227 |
| 9QTO | EM | 2.16 Å | A/B/C/D/E=24-349, A/B/C/D/E=455-502 |
| 8V8A | EM | 2.19 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 5AFJ | X-ray | 2.2 Å | A/B/C/D/E=23-227 |
| 9QTN | EM | 2.28 Å | A/B/C/D/E=24-502 |
| 8C9X | EM | 2.3 Å | A/B/C/D/E=24-347, A/B/C/D/E=455-502 |
| 8UT1 | EM | 2.3 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 8UTB | EM | 2.3 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 8UZJ | EM | 2.3 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 8V88 | EM | 2.3 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 8V80 | EM | 2.34 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 5AFK | X-ray | 2.38 Å | A/B/C/D/E=23-227 |
| 5AFL | X-ray | 2.38 Å | A/B/C/D/E=23-227 |
| 5AFH | X-ray | 2.4 Å | A/B/C/D/E=23-227 |
| 8V86 | EM | 2.47 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 8V89 | EM | 2.53 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 8V82 | EM | 2.61 Å | A/B/C/D/E=24-373, A/B/C/D/E=413-502 |
| 9LH5 | EM | 2.61 Å | A/B/C/D/E=1-502 |
| 9LH6 | EM | 2.69 Å | A/B/C/D/E=1-502 |
Showing 20 of 51 experimental structures (best resolution first).
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