Q86Y34: Adhesion G protein-coupled receptor G3 (ADGRG3)

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.

Gene
ADGRG3
Organism
Homo sapiens
Length
549 residues
Mean pLDDT
80.1
Model
AF-Q86Y34-F1 v6
Model created
1 Aug 2025
PDB structures
3

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate40%
70 to 90Confident: backbone generally right38%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

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…

Subunit structure

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)

Subcellular location

Cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
7D77EM2.9 ÅR=14-549
7D76EM3.1 ÅR=14-549
7QU8X-ray3.37 ÅA/B/C/D=1-264

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.