Small conductance calcium-activated potassium channel protein 2 (Kcnn2) is a 580-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P70604.
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The mean pLDDT of this model is 76.2 (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 | 42% |
| 70 to 90 | Confident: backbone generally right | 31% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Small 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:11325723, PubMed:20562108, PubMed:21422289, PubMed:8781233, PubMed:9774106). The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 3 picosiemens (PubMed:8781233, PubMed:9774106). Also presents an inwardly rectifying current, thus reducing its already small outward conductance of potassium ions, which is…
Homodimer (By similarity). Heteromultimer with KCNN1 and KCNN3 (By similarity). The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding (PubMed:11323678, PubMed:9774106). Interacts (via N-terminal domain) with MPP2 (By similarity)
Membrane, Cytoplasm, myofibril, sarcomere, Z line
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4J9Y | X-ray | 1.51 Å | B=396-487 |
| 1G4Y | X-ray | 1.6 Å | B=396-487 |
| 4G28 | X-ray | 1.63 Å | B=396-487 |
| 4G27 | X-ray | 1.65 Å | B=396-487 |
| 4J9Z | X-ray | 1.66 Å | B=396-487 |
| 3SJQ | X-ray | 1.9 Å | C/D=412-487 |
| 4QNH | X-ray | 2.02 Å | B=396-487 |
| 2PNV | X-ray | 2.1 Å | A/B=488-526 |
| 6CZQ | X-ray | 2.2 Å | B=395-487 |
| 9O7S | EM | 2.71 Å | A/B/C/D=118-478 |
| 9O93 | EM | 2.96 Å | A/B/C/D=121-500 |
| 1QX7 | X-ray | 3.09 Å | D=411-489 |
| 8V2H | EM | 3.1 Å | A/B/C/D=118-478 |
| 8V3G | EM | 3.1 Å | A/B/C/D=118-478 |
| 9O85 | EM | 3.13 Å | A/B/C/D=121-500 |
| 8V2G | EM | 3.18 Å | A/B/C/D=118-478 |
| 9EIO | EM | 3.62 Å | A/B/C/D=118-478 |
| 1KKD | NMR | A=396-487 |
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