Retinoic acid receptor RXR-alpha (RXRA) is a 462-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19793.
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The mean pLDDT of this model is 75.4 (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 | 54% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 30% |
What pLDDT means and how to read it
Receptor for retinoic acid that acts as a transcription factor (PubMed:10874028, PubMed:11162439, PubMed:11915042, PubMed:37478846). Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:16107141, PubMed:17761950, PubMed:18800767, PubMed:19167885, PubMed:28167758, PubMed:37478846). The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription (PubMed:10195690,…
Homodimer (PubMed:10669605, PubMed:17761950). Heterodimer (via C-terminus) with RARA; required for ligand-dependent retinoic acid receptor transcriptional activity; association with RARA is enhanced by pulsatile shear stress (PubMed:10698945, PubMed:15509776, PubMed:28167758). Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional…
Nucleus, Cytoplasm, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9QX6 | X-ray | 1.46 Å | A=229-462 |
| 6LB4 | X-ray | 1.5 Å | A=224-462 |
| 7A77 | X-ray | 1.5 Å | A=223-462 |
| 6FBQ | X-ray | 1.6 Å | A/B=130-212 |
| 9RMR | X-ray | 1.65 Å | A=229-462 |
| 1DSZ | X-ray | 1.7 Å | B=129-212 |
| 5MKU | X-ray | 1.78 Å | A=229-456 |
| 2P1T | X-ray | 1.8 Å | A=223-462 |
| 4ZSH | X-ray | 1.8 Å | A=223-462 |
| 6L6K | X-ray | 1.8 Å | A=224-462 |
| 7UW2 | X-ray | 1.88 Å | A=223-462 |
| 6STI | X-ray | 1.89 Å | A=223-462 |
| 1MV9 | X-ray | 1.9 Å | A=223-462 |
| 1MVC | X-ray | 1.9 Å | A=223-462 |
| 1MZN | X-ray | 1.9 Å | A/C/E/G=223-462 |
| 2NLL | X-ray | 1.9 Å | A=135-200 |
| 3E94 | X-ray | 1.9 Å | A=223-462 |
| 4RMD | X-ray | 1.9 Å | A=228-462 |
| 5MJ5 | X-ray | 1.9 Å | A=229-457 |
| 8PP0 | X-ray | 1.9 Å | A=223-462 |
Showing 20 of 110 experimental structures (best resolution first).
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