Parathyroid hormone/parathyroid hormone-related peptide receptor (PTH1R) is a 593-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q03431.
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The mean pLDDT of this model is 70.9 (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 | 35% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 30% |
What pLDDT means and how to read it
G protein-coupled receptor for parathyroid hormone (PTH) and for parathyroid hormone-related peptide (PTHLH) (PubMed:10913300, PubMed:11773434, PubMed:18375760, PubMed:19674967, PubMed:27160269, PubMed:30975883, PubMed:35932760, PubMed:8397094). 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 (cAMP) (PubMed:30975883, PubMed:35932760). PTH1R is coupled to G(s) G alpha proteins and mediates activation of adenylate cyclase activity (PubMed:20172855, PubMed:30975883, PubMed:35932760). PTHLH dissociates from PTH1R more rapidly than PTH; as…
Homodimer in the absence of bound ligand (PubMed:19674967, PubMed:20172855, PubMed:27160269, PubMed:30975883). Peptide hormone binding leads to dissociation of the homodimer (PubMed:19674967, PubMed:20172855)
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5EMB | X-ray | 0.85 Å | B=586-593 |
| 4Z8J | X-ray | 0.95 Å | B=586-593 |
| 7UZO | X-ray | 1.3 Å | A=30-174 |
| 3H3G | X-ray | 1.94 Å | A=29-187 |
| 3C4M | X-ray | 1.95 Å | A/B=29-187 |
| 8D51 | X-ray | 2.0 Å | A=29-174 |
| 8D52 | X-ray | 2.02 Å | A=29-174 |
| 7UZP | X-ray | 2.29 Å | A/C/E=29-174 |
| 8BIA | X-ray | 2.4 Å | C=586-593 |
| 6FJ3 | X-ray | 2.5 Å | A=24-388, A=398-480 |
| 8FLQ | EM | 2.55 Å | R=28-593 |
| 8JR9 | EM | 2.57 Å | R=27-502 |
| 8YG4 | EM | 2.59 Å | R=27-502 |
| 8BJ0 | X-ray | 2.6 Å | B=586-593 |
| 8HA0 | EM | 2.62 Å | R=27-502 |
| 8YFO | EM | 2.71 Å | R=27-502 |
| 8FLU | EM | 2.76 Å | R=28-593 |
| 7VVL | EM | 2.8 Å | R=27-491 |
| 7Y36 | EM | 2.8 Å | R=27-593 |
| 9JR2 | EM | 2.8 Å | R=27-593 |
Showing 20 of 40 experimental structures (best resolution first).
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