Voltage-dependent L-type calcium channel subunit alpha-1C (CACNA1C) is a 2221-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13936.
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The mean pLDDT of this model is 61.9 (low 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 | 11% |
| 70 to 90 | Confident: backbone generally right | 39% |
| 50 to 70 | Low: treat with caution | 16% |
| Below 50 | Very low: often disordered regions | 35% |
What pLDDT means and how to read it
Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:12181424, PubMed:15454078, PubMed:15863612, PubMed:16299511, PubMed:17224476, PubMed:20953164, PubMed:23677916, PubMed:24728418, PubMed:26253506, PubMed:27218670, PubMed:29078335, PubMed:29742403, PubMed:30023270, PubMed:30172029, PubMed:34163037, PubMed:8099908). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (PubMed:15454078, PubMed:15863612,…
Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta subunits (PubMed:12176756, PubMed:12181424, PubMed:15141227, PubMed:16299511, PubMed:20953164, PubMed:29078335, PubMed:29742403). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of subunit…
Cell membrane, Cell membrane, sarcolemma, Perikaryon, Postsynaptic density membrane, Cell projection, dendrite, Cell membrane, sarcolemma, T-tubule
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2F3Y | X-ray | 1.45 Å | B=1665-1685 |
| 2F3Z | X-ray | 1.6 Å | B=1665-1685 |
| 6DAD | X-ray | 1.65 Å | C/D=1659-1692 |
| 6U3A | X-ray | 1.65 Å | C/D=1659-1692 |
| 5V2Q | X-ray | 1.7 Å | B=427-445 |
| 6U3B | X-ray | 1.7 Å | B=1659-1692 |
| 6U3D | X-ray | 1.75 Å | C/D=1659-1692 |
| 1T0J | X-ray | 2.0 Å | C=428-445 |
| 2BE6 | X-ray | 2.0 Å | D/E/F=1659-1692 |
| 5V2P | X-ray | 2.0 Å | B=427-445 |
| 6DAE | X-ray | 2.0 Å | C/D=1659-1692 |
| 3G43 | X-ray | 2.1 Å | E/F=1609-1682 |
| 6DAF | X-ray | 2.4 Å | C/D=1659-1692 |
| 6U39 | X-ray | 2.4 Å | B/D/F/H/J/L/N/P/R/T=1659-1692 |
| 3OXQ | X-ray | 2.55 Å | E/F=1609-1685 |
| 8UKP | X-ray | 2.85 Å | C=1968-1984 |
| 8UKO | X-ray | 2.89 Å | C=1968-1984 |
| 8WE6 | EM | 2.9 Å | A=1-2221 |
| 8WE8 | EM | 2.9 Å | A=1-2221 |
| 8WE9 | EM | 3.0 Å | A=1-2221 |
Showing 20 of 33 experimental structures (best resolution first).
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