Q92847: Growth hormone secretagogue receptor type 1 (GHSR)

Growth hormone secretagogue receptor type 1 (GHSR) is a 366-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92847.

Gene
GHSR
Organism
Homo sapiens
Length
366 residues
Mean pLDDT
81.6
Model
AF-Q92847-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.6 (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 accurate51%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

G protein-coupled receptor specific to ghrelin, an appetite-regulating peptide hormone commonly found in stomach (PubMed:35027551, PubMed:39833471). Upon activation, stimulates appetite and promotes growth hormone secretion (PubMed:10604470, PubMed:11322507, PubMed:35027551, PubMed:39833471). Ghrelin binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as phospholipase C (By similarity). GHSR is coupled to G(q) G proteins and mediates production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (By similarity). Also binds other growth hormone releasing peptides…

Subunit structure

Interacts with the heterotrimeric G protein complex composed of 3 units, alpha, beta and gamma; this complex may consist of GNB1 and GNG2 (PubMed:35027551, PubMed:39833471). Interacts with DRD1; forms a heteromer with DRD1 in hippocampal neurons (By similarity). Interacts with DRD2; forms a heteromer with DRD2 in neurons (By similarity)

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
9UY3EM2.52 ÅR=1-366
9V2NEM2.63 ÅR=1-366
7NA7EM2.7 ÅR=1-366
7NA8EM2.7 ÅR=1-366
7W2ZEM2.8 ÅR=1-366
7F9YEM2.9 ÅR=1-366
8JSREM2.9 ÅR=2-366
7F83X-ray2.94 ÅA/B=35-243, A/B=253-342
7F9ZEM3.2 ÅR=1-366
6KO5X-ray3.3 ÅA=29-346

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