Sphingosine 1-phosphate receptor 1 (S1PR1) is a 382-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21453.
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The mean pLDDT of this model is 81.0 (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 | 54% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
G protein-coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular…
Interacts with GNAI1 and GNAI3. Interacts with CD69; this interaction promotes S1PR1 degradation (PubMed:37039481)
Cell membrane, Endosome, Membrane raft
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7TD4 | EM | 2.6 Å | R=2-382 |
| 9VNZ | EM | 2.79 Å | F=1-382 |
| 9VO0 | EM | 2.79 Å | F=1-382 |
| 3V2Y | X-ray | 2.8 Å | A=2-231, A=244-326 |
| 7VIF | EM | 2.83 Å | F=1-382 |
| 7EO4 | EM | 2.86 Å | A=1-382 |
| 7VIE | EM | 2.86 Å | F=1-382 |
| 7EO2 | EM | 2.89 Å | A=1-339 |
| 7VIG | EM | 2.89 Å | F=1-382 |
| 9VO1 | EM | 2.97 Å | F=1-382 |
| 7EVY | EM | 2.98 Å | D=1-337 |
| 7VIH | EM | 2.98 Å | F=1-382 |
| 7TD3 | EM | 3.0 Å | R=2-382 |
| 7EVZ | EM | 3.07 Å | D=1-337 |
| 8G94 | EM | 3.15 Å | A=1-347 |
| 7EW7 | EM | 3.27 Å | D=1-337 |
| 3V2W | X-ray | 3.35 Å | A=2-231, A=244-326 |
| 7WF7 | EM | 3.4 Å | A=1-382 |
| 7EW0 | EM | 3.42 Å | D=1-337 |
| 8YIC | EM | 3.47 Å | R=1-337 |
Showing 20 of 21 experimental structures (best resolution first).
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