Glucagon receptor (GCGR) is a 477-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P47871.
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The mean pLDDT of this model is 81.9 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 50% |
| 70 to 90 | Confident: backbone generally right | 32% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
G protein-coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:32193322, PubMed:38346960). Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system
Interacts with glucagon (PubMed:32193322). Interacts with GNAS (PubMed:32193322, PubMed:38346960). Interacts with GNAI1 (PubMed:32193322, PubMed:38346960)
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3CZF | X-ray | 1.2 Å | C=412-420 |
| 2A83 | X-ray | 1.4 Å | C=412-420 |
| 9N04 | EM | 2.3 Å | R=26-477 |
| 9N0E | EM | 2.3 Å | R=26-477 |
| 5EE7 | X-ray | 2.5 Å | A=136-254, A=259-417 |
| 4ERS | X-ray | 2.64 Å | A=28-123 |
| 8WG8 | EM | 2.71 Å | R=26-432 |
| 4LF3 | X-ray | 2.74 Å | C/F=29-123 |
| 8JIU | EM | 2.76 Å | R=27-431 |
| 8YW5 | EM | 2.84 Å | R=27-432 |
| 8FU6 | EM | 2.9 Å | R=27-477 |
| 8JIT | EM | 2.91 Å | R=27-431 |
| 5XEZ | X-ray | 3.0 Å | A/B=27-432 |
| 5YQZ | X-ray | 3.0 Å | R=27-257, R=260-432 |
| 9MZG | EM | 3.0 Å | R=26-477 |
| 9N1Q | EM | 3.0 Å | R=26-477 |
| 9N2I | EM | 3.0 Å | R=26-477 |
| 6WPW | EM | 3.1 Å | R=27-477 |
| 5XF1 | X-ray | 3.19 Å | A/B=27-256, A/B=260-432 |
| 4L6R | X-ray | 3.3 Å | A=123-434 |
Showing 20 of 27 experimental structures (best resolution first).
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