Q86SQ4: Adhesion G-protein coupled receptor G6 (ADGRG6)

Adhesion G-protein coupled receptor G6 (ADGRG6) is a 1221-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q86SQ4.

Gene
ADGRG6
Organism
Homo sapiens
Length
1221 residues
Mean pLDDT
73.8
Model
AF-Q86SQ4-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.8 (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 accurate16%
70 to 90Confident: backbone generally right54%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Adhesion G protein-coupled receptor (aGPCR) for steroid hormones, such as progesterone and 17alpha-hydroxyprogesterone (17OHP) (PubMed:35394864, PubMed:39884271). Involved in many biological processes, such as myelination, sprouting angiogenesis, placenta, ear and cartilage development (By similarity). 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:24227709, PubMed:35394864). ADGRG6 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:24227709, PubMed:35394864). Also able to couple to G(q) G…

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 Laminin-2; this interaction stabilizes the receptor in an inactive state (By similarity). Laminin-2 polymerization could facilitate ADGRG6-NTF removal, thereby…

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
21DUEM2.9 ÅR=578-1136

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