Acid-sensing ion channel 1 (ASIC1) is a 528-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P78348.
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The mean pLDDT of this model is 83.8 (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 | 61% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Forms voltage-independent, pH-gated trimeric sodium channels that act as postsynaptic excitatory receptors in the nervous system, playing a crucial role in regulating synaptic plasticity, learning, and memory (PubMed:21036899, PubMed:32915133, PubMed:34319232). Upon extracellular pH drop this channel elicits transient, fast activating, and completely desensitizing inward currents (PubMed:21036899). Displays high selectivity for sodium ions but can also permit the permeation of other cations (PubMed:21036899). Regulates more or less directly intracellular calcium concentration and CaMKII phosphorylation, and thereby the density of dendritic spines. Modulates neuronal activity in the…
Forms functional homotrimeric channels (PubMed:32915133, PubMed:34319232). Forms heterotrimers with other ASIC proteins, resulting in channels with distinct properties (PubMed:19654327). Interacts with PICK1; regulates ASIC1 clustering in membranes (PubMed:11802773, PubMed:12578970). Interacts with STOM; alters heterotrimeric channels activity (By similarity)
Cell membrane, Postsynaptic cell membrane, Cell projection, dendrite
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9E4I | EM | 2.33 Å | A/B/C=1-528 |
| 9E4H | EM | 2.61 Å | A/B/C=1-528 |
| 9E4F | EM | 2.69 Å | A/B/C=1-528 |
| 9E4A | EM | 2.74 Å | A/B/C=1-528 |
| 9E4K | EM | 2.77 Å | A/B/C=1-528 |
| 9E4G | EM | 2.8 Å | A/B/C=1-528 |
| 6L6N | X-ray | 2.86 Å | A/B/C=25-464 |
| 7RNN | EM | 2.86 Å | D=1-528 |
| 9E4J | EM | 2.87 Å | A/B/C=1-528 |
| 9E4B | EM | 3.09 Å | A/B/C=1-528 |
| 9E4E | EM | 3.16 Å | A/B/C=1-528 |
| 9E4D | EM | 3.19 Å | A/B/C=1-528 |
| 6L6I | X-ray | 3.24 Å | A/B/C=25-464 |
| 9E4C | EM | 3.41 Å | A/B/C=1-528 |
| 7CFS | EM | 3.56 Å | A/B/C=1-468 |
| 7CFT | EM | 3.9 Å | A/B/C=1-468 |
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