Adhesion G protein-coupled receptor G3 (ADGRG3) is a 549-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q86Y34.
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The mean pLDDT of this model is 80.1 (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 | 40% |
| 70 to 90 | Confident: backbone generally right | 38% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Adhesion G protein-coupled receptor (aGPCR) for glucocorticoid hormones such as cortisol, cortisone and 11-deoxycortisol (PubMed:33408414). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:33408414). ADGRG3/GPR97 is coupled to G(o)/GNAO1 G proteins and mediates signaling by inhibiting adenylate cyclase activity (PubMed:33408414). May also signal through G-alpha(q)-proteins; additional evidence are however required to confirm this result in vivo (PubMed:22575658). Plays a role in the regulation of various processes including B-cell…
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 with PRTN3; this interaction induces the activation of PAR2 (PubMed:36302784). Interacts with GNAO1 (when palmitoylated) (PubMed:33408414)
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7D77 | EM | 2.9 Å | R=14-549 |
| 7D76 | EM | 3.1 Å | R=14-549 |
| 7QU8 | X-ray | 3.37 Å | A/B/C/D=1-264 |
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