TGF-beta receptor type-1 (TGFBR1) is a 503-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P36897.
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The mean pLDDT of this model is 84.2 (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 | 62% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis (PubMed:33914044). The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the…
Homodimer; in the endoplasmic reticulum but also at the cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different…
Cell membrane, Cell junction, tight junction, Cell surface, Membrane raft
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9J9D | X-ray | 1.34 Å | A=200-503 |
| 8YHF | X-ray | 1.4 Å | A=162-503 |
| 5E8S | X-ray | 1.45 Å | A=200-503 |
| 5E8X | X-ray | 1.45 Å | A=200-503 |
| 8YHL | X-ray | 1.47 Å | A=200-503 |
| 4X2F | X-ray | 1.49 Å | A=200-503 |
| 4X2G | X-ray | 1.51 Å | A=200-503 |
| 5E8Z | X-ray | 1.51 Å | A=200-503 |
| 5QIK | X-ray | 1.58 Å | A=200-503 |
| 6B8Y | X-ray | 1.65 Å | A=200-503 |
| 5QU0 | X-ray | 1.67 Å | A=200-503 |
| 4X0M | X-ray | 1.68 Å | A=200-503 |
| 4X2J | X-ray | 1.69 Å | A=200-503 |
| 4X2K | X-ray | 1.69 Å | A=200-503 |
| 3HMM | X-ray | 1.7 Å | A=201-503 |
| 3TZM | X-ray | 1.7 Å | A=200-503 |
| 5E8T | X-ray | 1.7 Å | A=200-503 |
| 5QIM | X-ray | 1.75 Å | A=200-503 |
| 3GXL | X-ray | 1.8 Å | A=201-503 |
| 4X2N | X-ray | 1.8 Å | A=200-503 |
Showing 20 of 44 experimental structures (best resolution first).
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