Rhodopsin (RHO) is a 348-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02699.
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The mean pLDDT of this model is 89.8 (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 | 78% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
G protein-coupled photoreceptor that activates the G protein transducin (t) signaling pathway in response to light and is essential for image-forming vision under low-light conditions (PubMed:31300275). Required for postnatal photoreceptor cell viability (By similarity). Activation occurs when the covalently bound 11-cis-retinal chromophore absorbs a photon and isomerizes to all-trans-retinal, inducing a conformational change in the opsin that triggers G protein-mediated phototransduction (Probable) (PubMed:16586416, PubMed:16908857, PubMed:17060607, PubMed:17449675, PubMed:18818650, PubMed:21389983, PubMed:22198838, PubMed:23579341, PubMed:25205354, PubMed:27458239, PubMed:31300275).…
Homodimer (PubMed:18563085, PubMed:23303210). May form a complex composed of RHO, GRK1 and RCVRN in a Ca(2+)-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (PubMed:17020884). Interacts with GRK1 (By similarity). Interacts (phosphorylated form) with SAG (PubMed:15111114, PubMed:15351781, PubMed:23579341, PubMed:25205354, PubMed:26200343). Interacts with GNAT1…
Photoreceptor outer segment membrane, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7ZBC | X-ray | 1.8 Å | A/B=1-348 |
| 7ZBE | X-ray | 1.8 Å | A/B=1-348 |
| 8A6C | X-ray | 1.8 Å | A/B=1-348 |
| 8A6D | X-ray | 1.8 Å | A/B=1-348 |
| 8A6E | X-ray | 1.8 Å | A/B=1-348 |
| 1U19 | X-ray | 2.2 Å | A/B=1-348 |
| 4X1H | X-ray | 2.29 Å | A=1-348 |
| 5DYS | X-ray | 2.3 Å | A=1-348 |
| 6FK6 | X-ray | 2.36 Å | A=1-326 |
| 6FKC | X-ray | 2.46 Å | A=1-348 |
| 6FKD | X-ray | 2.49 Å | A=1-348 |
| 1L9H | X-ray | 2.6 Å | A/B=1-348 |
| 2G87 | X-ray | 2.6 Å | A/B=1-348 |
| 3OAX | X-ray | 2.6 Å | A/B=1-348 |
| 6FK7 | X-ray | 2.62 Å | A=1-348 |
| 6FK9 | X-ray | 2.63 Å | A=1-348 |
| 1GZM | X-ray | 2.65 Å | A/B=1-348 |
| 3C9L | X-ray | 2.65 Å | A=1-348 |
| 4J4Q | X-ray | 2.65 Å | A=1-348 |
| 8RJB | EM | 2.69 Å | B=32-109 |
Showing 20 of 78 experimental structures (best resolution first).
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