Voltage-gated inwardly rectifying potassium channel KCNH2 (KCNH2) is a 1159-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12809.
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The mean pLDDT of this model is 62.8 (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 | 27% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 45% |
What pLDDT means and how to read it
Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel (PubMed:10219239, PubMed:10753933, PubMed:10790218, PubMed:10837251, PubMed:11997281, PubMed:12063277, PubMed:18559421, PubMed:22314138, PubMed:22359612, PubMed:26363003, PubMed:27916661, PubMed:9230439, PubMed:9351446, PubMed:9765245). Channel properties are modulated by cAMP and subunit assembly (PubMed:10837251). Characterized by unusual gating kinetics by producing relatively small outward currents during membrane depolarization and large inward currents during subsequent repolarization which reflect a rapid inactivation during depolarization and quick recovery from inactivation but slow deactivation…
The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits (PubMed:27916661). Interacts with DNAJB12 and DNAJB14; chaperones DNAJB12 and DNAJB14 promote tetramerization (PubMed:27916661). Heteromultimer with KCNH6/ERG2 and KCNH7/ERG3 (By similarity). Interacts with ALG10B (By similarity). Forms…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6SYG | X-ray | 1.5 Å | A=734-864 |
| 4HQA | X-ray | 1.96 Å | A=1-135 |
| 4HP9 | X-ray | 2.12 Å | A=10-135 |
| 1BYW | X-ray | 2.6 Å | A=26-135 |
| 9CHQ | EM | 3.0 Å | A/B/C/D=1-1159 |
| 8ZYQ | EM | 3.18 Å | A/B/C/D=1-1159 |
| 8ZYP | EM | 3.19 Å | A/B/C/D=1-1159 |
| 8ZYN | EM | 3.27 Å | A/B/C/D=1-1159 |
| 8ZYO | EM | 3.29 Å | A/B/C/D=1-1159 |
| 9CHP | EM | 3.3 Å | A/B/C/D=1-1159 |
| 9CHS | EM | 3.4 Å | A/B/C/D=1-1159 |
| 8IO4 | EM | 3.5 Å | A/B/C/D=1-1159 |
| 9CHR | EM | 3.5 Å | A/B/C/D=1-1159 |
| 5VA1 | EM | 3.7 Å | A=1-1159 |
| 5VA2 | EM | 3.8 Å | A=1-1159 |
| 8IO5 | EM | 3.8 Å | A/B/C/D=1-1159 |
| 8IOB | EM | 3.9 Å | A/B/C/D=1-1159 |
| 5VA3 | EM | 4.0 Å | A=1-1159 |
| 1UJL | NMR | A=570-611 | |
| 2L0W | NMR | A=1-135 |
Showing 20 of 24 experimental structures (best resolution first).
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