Adhesion G protein-coupled receptor L3 (Adgrl3) is a 1537-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q80TS3.
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The mean pLDDT of this model is 67.2 (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 | 30% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 35% |
What pLDDT means and how to read it
Orphan adhesion G protein-coupled receptor (aGPCR), which mediates synapse specificity (PubMed:36244455, PubMed:38233523). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:36244455, PubMed:36309016). ADGRL3 is coupled with different classes of G alpha proteins, such as G(12)/G(13), G(s), G(i) or G(q), depending on the context (PubMed:32778842, PubMed:36309016, PubMed:39798870). Coupling to G(12)/G(13) G proteins, which mediates the activation Rho small GTPases is the most efficient (PubMed:32778842, PubMed:36244455). Following G protein-coupled receptor…
Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked (By similarity). Interacts (via olfactomedin-like domain) with FLRT1 (via extracellular domain) (PubMed:22405201). Interacts (via olfactomedin-like domain) with FLRT2 (via extracellular…
Cell membrane, Postsynaptic cell membrane, Cell projection, axon, Cell junction
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4RML | X-ray | 1.6 Å | A=199-495 |
| 4RMK | X-ray | 1.61 Å | A=199-495 |
| 6JBU | X-ray | 1.85 Å | A=203-461 |
| 5AFB | X-ray | 2.16 Å | A=97-459 |
| 7WY5 | EM | 2.83 Å | R=1-1537 |
| 7WY8 | EM | 2.83 Å | R=1-1537 |
| 7X10 | EM | 2.93 Å | R=1-1537 |
| 7WYB | EM | 2.97 Å | R=1-1537 |
| 4YEB | X-ray | 3.19 Å | A=199-495 |
| 5FTT | X-ray | 3.4 Å | C/D/G/H=92-463 |
| 5FTU | X-ray | 6.01 Å | C/D/G/H/K/L=92-463 |
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