Q9Y653: Adhesion G-protein coupled receptor G1 (ADGRG1)

Adhesion G-protein coupled receptor G1 (ADGRG1) is a 693-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y653.

Gene
ADGRG1
Organism
Homo sapiens
Length
693 residues
Mean pLDDT
77.9
Model
AF-Q9Y653-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.9 (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 accurate27%
70 to 90Confident: backbone generally right49%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

Adhesion G protein-coupled receptor (aGPCR) for steroid hormone 17alpha-hydroxypregnenolone (17-OH), which is involved in cell adhesion and cell-cell interactions (PubMed:39389061). 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 RhoA pathway (PubMed:28874577, PubMed:35418682, PubMed:39389061). ADGRG1 is coupled to G(12) and/or G(13) G proteins (GNA12 and GNA13, respectively) and mediates the activation Rho small GTPases (PubMed:22238662, PubMed:28424266, PubMed:35418682, PubMed:39389061). Acts as a potent suppressor of ferroptosis: binding to 17-OH-binding…

Subunit structure

Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment (ADGRG1 NT) and the membrane-bound C-terminal fragment (ADGRG1-CT) predominantly remain associated and non-covalently linked (PubMed:22333914). ADGRG1 NT self-associates in a trans-trans manner; the homophilic interaction enhances receptor signaling (PubMed:21708946). Interacts with TGM2…

Subcellular location

Cell membrane, Secreted, Membrane raft

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7SF8EM2.7 ÅA=383-693

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