Activin receptor type-1 (ACVR1) is a 509-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q04771.
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The mean pLDDT of this model is 83.1 (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 | 57% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Bone morphogenetic protein (BMP) type I receptor that is involved in a wide variety of biological processes, including bone, heart, cartilage, nervous, and reproductive system development and regulation (PubMed:20628059, PubMed:22977237). As a type I receptor, forms heterotetrameric receptor complexes with the type II receptors AMHR2, ACVR2A or ACVR2B (PubMed:17911401). Upon binding of ligands such as BMP7 or GDF2/BMP9 to the heteromeric complexes, type II receptors transphosphorylate ACVR1 intracellular domain (PubMed:25354296). In turn, ACVR1 kinase domain is activated and subsequently phosphorylates SMAD1/5/8 proteins that transduce the signal (PubMed:9748228). In addition to its role…
Interacts with FKBP1A (PubMed:22484487, Ref.14). Interacts with FCHO1 (PubMed:22484487). Interacts with CLU (PubMed:8555189). Interacts with type II receptors AMHR2 and ACVR2A (PubMed:17911401). Interacts with BMP7 (PubMed:9748228). Interacts with GDF2/BMP9 (PubMed:20628059). Interacts with BMP6 (when glycosylated); the interaction may induce HAMP expression (PubMed:18070108, PubMed:31800957).…
Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6SRH | X-ray | 1.25 Å | A/B=201-499 |
| 5S75 | X-ray | 1.3 Å | A/B=201-499 |
| 5S78 | X-ray | 1.3 Å | A/B=201-499 |
| 5S7A | X-ray | 1.3 Å | A/B=201-499 |
| 5S7H | X-ray | 1.3 Å | A/B=201-499 |
| 5S7I | X-ray | 1.3 Å | A/B=201-499 |
| 5S7N | X-ray | 1.3 Å | A/B=201-499 |
| 5S7S | X-ray | 1.3 Å | A/B=201-499 |
| 5S7T | X-ray | 1.3 Å | A/B=201-499 |
| 5S7X | X-ray | 1.3 Å | A/B=201-499 |
| 5S7Z | X-ray | 1.3 Å | A/B=201-499 |
| 5S87 | X-ray | 1.3 Å | A/B=201-499 |
| 5S89 | X-ray | 1.3 Å | A/B=201-499 |
| 5S8A | X-ray | 1.3 Å | A/B=201-499 |
| 5S76 | X-ray | 1.31 Å | A/B=201-499 |
| 5S77 | X-ray | 1.31 Å | A/B=201-499 |
| 5S7C | X-ray | 1.31 Å | A/B=201-499 |
| 5S7D | X-ray | 1.31 Å | A/B=201-499 |
| 5S7F | X-ray | 1.31 Å | A/B=201-499 |
| 5S7J | X-ray | 1.31 Å | A/B=201-499 |
Showing 20 of 85 experimental structures (best resolution first).
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