Cannabinoid receptor 1 (CNR1) is a 472-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21554.
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The mean pLDDT of this model is 71.7 (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 | 48% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 14% |
| Below 50 | Very low: often disordered regions | 27% |
What pLDDT means and how to read it
G protein-coupled receptor for endogenous cannabinoids (eCBs), including N-arachidonoylethanolamide (also called anandamide or AEA) and 2-arachidonoylglycerol (2-AG), as well as phytocannabinoids, such as delta(9)-tetrahydrocannabinol (THC) (PubMed:15620723, PubMed:27768894, PubMed:27851727, PubMed:35637350). Mediates many cannabinoid-induced effects, acting, among others, on food intake, memory loss, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, chronic pain. Signaling typically involves reduction in cyclic AMP (PubMed:1718258, PubMed:21895628, PubMed:27768894). In the hypothalamus, may have a dual effect on mitochondrial respiration depending upon the agonist dose…
Interacts (via C-terminus) with CNRIP1; this interaction attenuates constitutive, but not agonist-dependent, inhibition of voltage-gated Ca(2+) channels in neurons (PubMed:17895407). Associates with G protein alpha subunits, including G(i) alpha-1/GNAI1, G(i) alpha-2/GNAI2, G(i) alpha-3/GNAI3 and G(o)-alpha/GNAO1; palmitoylation is important for interaction with GNAI3 and GNAO1 (PubMed:12237474)
Cell membrane, Membrane raft, Mitochondrion outer membrane, Cell projection, axon, Presynapse
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5U09 | X-ray | 2.6 Å | A=90-301, A=334-421 |
| 7FEE | X-ray | 2.7 Å | A=74-305, A=333-414 |
| 5TGZ | X-ray | 2.8 Å | A=99-306, A=332-414 |
| 5XRA | X-ray | 2.8 Å | A=99-306, A=332-414 |
| 8GHV | EM | 2.8 Å | D=1-472 |
| 9B54 | EM | 2.86 Å | R=1-472 |
| 8K8J | EM | 2.88 Å | R=71-425 |
| 9ERX | EM | 2.9 Å | R=2-472 |
| 5XR8 | X-ray | 2.95 Å | A=99-306, A=332-414 |
| 6KPG | EM | 3.0 Å | R=71-425 |
| 6N4B | EM | 3.0 Å | R=1-472 |
| 9B65 | EM | 3.03 Å | R=1-472 |
| 9BA0 | EM | 3.13 Å | R=96-301, R=334-416 |
| 8WU1 | EM | 3.2 Å | R=1-413 |
| 9EGO | EM | 3.2 Å | R=1-472 |
| 6KQI | X-ray | 3.25 Å | A=94-301, A=334-413 |
| 7V3Z | X-ray | 3.29 Å | A=102-306, A=336-414 |
| 8GAG | EM | 3.3 Å | R=1-472 |
| 8IKH | EM | 3.3 Å | R=99-408 |
| 9B9Z | EM | 3.3 Å | R=96-301, R=334-416 |
Showing 20 of 32 experimental structures (best resolution first).
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