Disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) is a 824-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P78536.
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The mean pLDDT of this model is 72.7 (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 | 25% |
| 70 to 90 | Confident: backbone generally right | 42% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins including adhesion proteins, growth factor precursors and cytokines important for inflammation and immunity (PubMed:24226769, PubMed:24227843, PubMed:28060820, PubMed:28923481, PubMed:38771644). Cleaves the membrane-bound precursor of TNF to its mature soluble form (PubMed:36078095, PubMed:9034191). Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth…
Interacts with MAD2L1, MAPK14 and MUC1 (PubMed:12441351, PubMed:20188673). Interacts with iRhom1/RHBDF1 and iRhom2/RHBDF2 (PubMed:29897333). Interacts with FRMD8 via its interaction with iRhom1/RHBDF1 and iRhom2/RHBDF2 (PubMed:29897333). Interacts with TSPAN8 (PubMed:36078095)
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2DDF | X-ray | 1.7 Å | A/B=218-474 |
| 8CQY | X-ray | 1.7 Å | B=813-824 |
| 3L0V | X-ray | 1.75 Å | A/B=215-476 |
| 3EWJ | X-ray | 1.8 Å | A/B=215-477 |
| 3KMC | X-ray | 1.8 Å | A/B=215-476 |
| 3KME | X-ray | 1.85 Å | A/B=215-476 |
| 3LE9 | X-ray | 1.85 Å | A/B=215-476 |
| 3O64 | X-ray | 1.88 Å | A/B=215-476 |
| 2I47 | X-ray | 1.9 Å | A/B/C/D=212-493 |
| 3E8R | X-ray | 1.9 Å | A/B=215-477 |
| 3EDZ | X-ray | 1.9 Å | A/B=215-477 |
| 3LGP | X-ray | 1.9 Å | A/B=215-476 |
| 3L0T | X-ray | 1.92 Å | A/B=215-476 |
| 1BKC | X-ray | 2.0 Å | A/C/E/I=219-474 |
| 2OI0 | X-ray | 2.0 Å | A=216-477 |
| 3B92 | X-ray | 2.0 Å | A=216-474 |
| 3LEA | X-ray | 2.0 Å | A/B=215-476 |
| 2FV9 | X-ray | 2.02 Å | A/B=218-475 |
| 2FV5 | X-ray | 2.1 Å | A/B=216-475 |
| 3G42 | X-ray | 2.1 Å | A/B/C/D=212-492 |
Showing 20 of 31 experimental structures (best resolution first).
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