Receptor-interacting serine/threonine-protein kinase 1 (RIPK1) is a 671-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13546.
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The mean pLDDT of this model is 69.8 (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 | 32% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 31% |
What pLDDT means and how to read it
Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways (PubMed:17703191, PubMed:24144979, PubMed:31827280, PubMed:31827281, PubMed:32657447, PubMed:35831301). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part,…
Homodimer (PubMed:29440439, PubMed:29681455). Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necroptosis-inducing complex (PubMed:10358032, PubMed:11734559, PubMed:19524512, PubMed:29681455, PubMed:29883609). Upon TNF-induced necrosis, the RIPK1-RIPK3 dimer further…
Cytoplasm, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5ZMZ | X-ray | 1.4 Å | A=539-542 |
| 6AC5 | X-ray | 1.45 Å | A=561-671 |
| 4ITJ | X-ray | 1.8 Å | A/B=1-294 |
| 6NW2 | X-ray | 2.0 Å | A/B=1-294 |
| 7FD0 | X-ray | 2.0 Å | A/B=1-294 |
| 24IB | X-ray | 2.05 Å | A/B=1-294 |
| 9Q31 | X-ray | 2.05 Å | A/B=1-294 |
| 6NYH | X-ray | 2.1 Å | A/B=1-294 |
| 9GTY | X-ray | 2.15 Å | A/B=1-294 |
| 7FCZ | X-ray | 2.21 Å | A/B=1-294 |
| 5HX6 | X-ray | 2.23 Å | A/B=1-294 |
| 4ITH | X-ray | 2.25 Å | A/B=1-294 |
| 9GTG | X-ray | 2.25 Å | A/B=1-294 |
| 8I2N | X-ray | 2.29 Å | A/B=1-294 |
| 9HY9 | X-ray | 2.29 Å | A/B=1-294 |
| 9MZY | X-ray | 2.32 Å | A/B=8-294 |
| 7XMK | X-ray | 2.38 Å | A/B=1-294 |
| 9Q32 | X-ray | 2.49 Å | A/B/C/D=1-294 |
| 6C4D | X-ray | 2.52 Å | A/B/C/D=2-294 |
| 9MZX | X-ray | 2.53 Å | A/B=6-294 |
Showing 20 of 39 experimental structures (best resolution first).
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