Potassium voltage-gated channel subfamily KQT member 2 (KCNQ2) is a 872-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43526.
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The mean pLDDT of this model is 58.2 (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 | 21% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 53% |
What pLDDT means and how to read it
Pore-forming subunit of the voltage-gated potassium (Kv) M-channel which is responsible for the M-current, a key controller of neuronal excitability (PubMed:24277843, PubMed:28793216, PubMed:9836639). M-channel is composed of pore-forming subunits KCNQ2 and KCNQ3 assembled as heterotetramers (PubMed:10781098, PubMed:14534157, PubMed:32884139, PubMed:37857637, PubMed:9836639). The native M-current has a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs (PubMed:14534157, PubMed:28793216, PubMed:9836639). KCNQ2-KCNQ3 M-channel is selectively…
Heterotetramer with KCNQ3; forms heterotetrameric M-channel responsible for the native M-current (PubMed:10781098, PubMed:27564677, PubMed:9836639). Homotetrameric; forms a functional homotetrameric channel resulting in the expression of a small M-current (PubMed:32884139, PubMed:37857637, PubMed:9836639). Interacts with calmodulin; the interaction is calcium-independent, constitutive and…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5J03 | X-ray | 2.0 Å | A=530-557 |
| 8IZY | EM | 2.5 Å | A/B/C/D=64-702 |
| 8J03 | EM | 2.7 Å | A/D/G/I=64-703 |
| 8J04 | EM | 2.7 Å | A/B/D/G=64-702 |
| 8J05 | EM | 2.7 Å | A/B/D/G=64-702 |
| 9L8W | EM | 2.9 Å | A/B/C/D=1-872 |
| 8J00 | EM | 3.0 Å | A/B/C/D=64-702 |
| 8X43 | EM | 3.0 Å | A/C/E/G=64-702 |
| 7CR0 | EM | 3.1 Å | A/B/C/D=64-702 |
| 8J01 | EM | 3.1 Å | A/B/D/G=64-702 |
| 9IXY | EM | 3.1 Å | A/B/C/D=64-702 |
| 9XB9 | EM | 3.1 Å | A/B/C/D=1-872 |
| 7CR2 | EM | 3.2 Å | A/B/C/D=64-702 |
| 9IXZ | EM | 3.2 Å | A/B/C/D=64-702 |
| 8W4U | EM | 3.3 Å | A/B/D/G=64-702 |
| 7CR1 | EM | 3.4 Å | A/B/C/D=64-702 |
| 8IJK | EM | 3.4 Å | A/B/C/D=64-702 |
| 9XED | EM | 3.4 Å | A/B/C/D=1-872 |
| 8J02 | EM | 3.5 Å | A/B/D/G=64-703 |
| 7CR3 | EM | 3.6 Å | A/B/D/G=64-702 |
Showing 20 of 25 experimental structures (best resolution first).
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