Mu-type opioid receptor (OPRM1) is a 400-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35372.
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The mean pLDDT of this model is 76.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 48% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 18% |
What pLDDT means and how to read it
Receptor for endogenous opioids such as beta-endorphin and endomorphin (PubMed:10529478, PubMed:12589820, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed:10529478, PubMed:10836142, PubMed:12589820, PubMed:19300905, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (By similarity). Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G protein complex and…
Forms homooligomers and heterooligomers with other GPCRs, such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5 (probably in dimeric forms) (PubMed:12413885, PubMed:15778451, PubMed:15967873, PubMed:17224450). Interacts with heterotrimeric G proteins; interaction with a heterotrimeric complex containing GNAI1, GNB1 and GNG2 stabilizes the active conformation of the receptor and…
Cell membrane, Cell projection, axon, Perikaryon, Cell projection, dendrite, Endosome, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8Y72 | EM | 2.65 Å | R=2-388 |
| 9PY4 | EM | 2.78 Å | R=2-400 |
| 8EFO | EM | 2.8 Å | M/R=2-368 |
| 9WST | EM | 2.8 Å | R=7-400 |
| 8Y73 | EM | 2.84 Å | R=2-388 |
| 8K9K | EM | 2.98 Å | R=64-362 |
| 9PXY | EM | 3.0 Å | R=2-400 |
| 9PXV | EM | 3.02 Å | R=2-400 |
| 8K9L | EM | 3.05 Å | R=64-362 |
| 9PXX | EM | 3.1 Å | R=2-400 |
| 9PY2 | EM | 3.16 Å | R=2-400 |
| 8EF6 | EM | 3.2 Å | M/R=2-368 |
| 8EFB | EM | 3.2 Å | R=2-368 |
| 8EFL | EM | 3.2 Å | M/R=2-368 |
| 9PY3 | EM | 3.2 Å | R=2-400 |
| 8F7Q | EM | 3.22 Å | M/R=2-388 |
| 9MQJ | EM | 3.23 Å | A=1-400 |
| 8F7R | EM | 3.28 Å | M/R=2-388 |
| 8EF5 | EM | 3.3 Å | M/R=2-368 |
| 8EFQ | EM | 3.3 Å | R=2-368 |
Showing 20 of 25 experimental structures (best resolution first).
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