Cystic fibrosis transmembrane conductance regulator (CFTR) is a 1480-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13569.
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The mean pLDDT of this model is 75.6 (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 | 32% |
| 70 to 90 | Confident: backbone generally right | 42% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:10792060, PubMed:11524016, PubMed:11707463, PubMed:12519745, PubMed:12529365, PubMed:12588899, PubMed:12727866, PubMed:15010471, PubMed:17036051, PubMed:1712898, PubMed:17182731, PubMed:19398555, PubMed:19621064, PubMed:22178883, PubMed:25330774, PubMed:26846474, PubMed:28087700, PubMed:8910473, PubMed:9804160). Possesses an intrinsic ATPase activity and utilizes ATP to gate its channel; the passive flow of anions through the channel is gated by cycles of ATP binding and…
Monomer; does not require oligomerization for channel activity (PubMed:11524016). May form oligomers in the membrane (PubMed:11524016). Interacts with SLC26A3, SLC26A6 and SHANK2 (By similarity). Interacts with NHERF1 and MYO6 (PubMed:11304524, PubMed:12403779, PubMed:15247260). Interacts (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR internalization and thereby decreases…
Apical cell membrane, Early endosome membrane, Cell membrane, Recycling endosome membrane, Endoplasmic reticulum membrane, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2PZE | X-ray | 1.7 Å | A/B=387-646 |
| 7QI1 | X-ray | 1.76 Å | E/F=747-774 |
| 2PZG | X-ray | 1.8 Å | A/B=375-646 |
| 5TFJ | X-ray | 1.85 Å | A=387-646 |
| 5TF8 | X-ray | 1.86 Å | A=387-646 |
| 6HEP | X-ray | 1.86 Å | E/F=747-774 |
| 6WBS | X-ray | 1.86 Å | A/B=388-646 |
| 5TFA | X-ray | 1.87 Å | A=387-646 |
| 5TFB | X-ray | 1.87 Å | A=387-646 |
| 5TFD | X-ray | 1.89 Å | A=387-646 |
| 5TFF | X-ray | 1.89 Å | A=387-646 |
| 5TFI | X-ray | 1.89 Å | A=387-646 |
| 5TFG | X-ray | 1.91 Å | A=387-646 |
| 5TGK | X-ray | 1.91 Å | A=387-646 |
| 5TFC | X-ray | 1.92 Å | A=387-646 |
| 5TF7 | X-ray | 1.93 Å | A=387-646 |
| 6GJS | X-ray | 1.95 Å | A=387-646 |
| 2PZF | X-ray | 2.0 Å | A/B=387-646 |
| 2BBS | X-ray | 2.05 Å | A/B=388-678 |
| 4WZ6 | X-ray | 2.05 Å | A=389-678 |
Showing 20 of 58 experimental structures (best resolution first).
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