Intermediate conductance calcium-activated potassium channel protein 4 (KCNN4) is a 427-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15554.
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The mean pLDDT of this model is 84.2 (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 | 51% |
| 70 to 90 | Confident: backbone generally right | 36% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Intermediate conductance calcium-activated potassium channel that mediates the voltage-independent transmembrane transfer of potassium across the cell membrane through a constitutive interaction with calmodulin which binds the intracellular calcium allowing its opening (PubMed:10026195, PubMed:10961988, PubMed:11425865, PubMed:15831468, PubMed:17157250, PubMed:18796614, PubMed:26148990, PubMed:9326665, PubMed:9380751, PubMed:9407042). The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 25 picosiemens (PubMed:9326665, PubMed:9380751, PubMed:9407042). Also presents an…
Homodimer (PubMed:29953543). Homotetramer (PubMed:29724949). Heterotetramer of potassium channel proteins (Probable). Interacts with MTMR6; this interaction leads to selective dephosphorylation of PI(3)P in a lipid microdomain adjacent to KCNN4, resulting in a decrease of intermediate conductance calcium-activated potassium channel activity (PubMed:15831468). Interacts (via the C-tail domain)…
Cell membrane, Cell projection, ruffle membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6D42 | X-ray | 1.75 Å | A/B=376-415 |
| 9ZRK | EM | 2.99 Å | A/B/C/D=9-386 |
| 9O48 | EM | 3.1 Å | A/B/C/D=1-15, A/B/C/D=305-427 |
| 9O5O | EM | 3.1 Å | A/B/C/D=1-15, A/B/C/D=305-427 |
| 9O52 | EM | 3.18 Å | A/B/C/D=1-15, A/B/C/D=305-427 |
| 9O53 | EM | 3.3 Å | A/B/C/D=1-15, A/B/C/D=305-427 |
| 9ZRL | EM | 3.38 Å | A/B/C/D=9-369 |
| 9ZPT | EM | 3.39 Å | A/B/C/D=9-366 |
| 6CNM | EM | 3.4 Å | A/B/C/D=1-427 |
| 9O51 | EM | 3.4 Å | A/B/C/D=1-15, A/B/C/D=305-427 |
| 9YDZ | EM | 3.4 Å | A/B/C/D=9-366 |
| 6CNN | EM | 3.5 Å | A/B/C/D=1-427 |
| 9ED1 | EM | 3.5 Å | A/B/C/D=9-386 |
| 9OA8 | EM | 3.59 Å | A/B/C/D=9-386 |
| 9ZPO | EM | 3.67 Å | A/B/C/D=9-386 |
| 6CNO | EM | 4.7 Å | A/B/C/D=1-427 |
| 9Y5Q | EM | 4.73 Å | A/B/C/D=9-386 |
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