Calcitonin gene-related peptide type 1 receptor (CALCRL) is a 461-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16602.
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The mean pLDDT of this model is 78.7 (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 | 41% |
| 70 to 90 | Confident: backbone generally right | 34% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
G protein-coupled receptor which specificity is determined by its interaction with receptor-activity-modifying proteins (RAMPs) (PubMed:32296767, PubMed:33602864, PubMed:8626685). Together with RAMP1, form the receptor complex for calcitonin-gene-related peptides CALCA/CGRP1 and CALCB/CGRP2 (PubMed:33602864). Together with RAMP2 or RAMP3, function as receptor complexes for adrenomedullin (ADM and ADM2) (PubMed:32296767, PubMed:9620797). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors. Activates cAMP-dependent pathway (PubMed:32296767, PubMed:8626685)
Heterodimer of CALCRL and RAMP1; the receptor complex functions as CGRP receptor (PubMed:20826335, PubMed:33602864). Heterodimer of CALCRL and RAMP2 or CALCRL and RAMP3; the complexes function as adrenomedullin receptor (PubMed:22102369, PubMed:30115739, PubMed:32296767)
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6ZHO | X-ray | 1.6 Å | A=29-144 |
| 8AX7 | X-ray | 1.65 Å | A=29-144 |
| 6ZIS | X-ray | 1.73 Å | A=31-139 |
| 4RWF | X-ray | 1.76 Å | A=31-144 |
| 6V2E | X-ray | 1.83 Å | A=29-144 |
| 7P0F | X-ray | 1.85 Å | A=29-144 |
| 8AX6 | X-ray | 1.9 Å | A=29-144 |
| 6D1U | X-ray | 2.05 Å | A/B/C=29-144 |
| 3N7S | X-ray | 2.1 Å | A/B=23-133 |
| 6UVA | EM | 2.3 Å | R=22-461 |
| 7P0I | X-ray | 2.3 Å | A=29-144 |
| 6UUS | EM | 2.4 Å | R=22-461 |
| 4RWG | X-ray | 2.44 Å | A/B/C=31-144 |
| 3AQF | X-ray | 2.6 Å | B=23-136 |
| 6UMG | X-ray | 2.7 Å | C/c=23-133 |
| 8AX5 | X-ray | 2.75 Å | A=29-144 |
| 3N7P | X-ray | 2.8 Å | A/B/C/J=23-133 |
| 5V6Y | X-ray | 2.8 Å | A/B/C/D=29-144 |
| 3N7R | X-ray | 2.9 Å | A/B=23-133 |
| 6UUN | EM | 3.0 Å | R=22-461 |
Showing 20 of 25 experimental structures (best resolution first).
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