Bile acid receptor (NR1H4) is a 486-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96RI1.
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The mean pLDDT of this model is 68.8 (low 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 | 36% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 33% |
What pLDDT means and how to read it
Ligand-activated transcription factor. Receptor for bile acids (BAs) such as chenodeoxycholic acid (CDCA), lithocholic acid, deoxycholic acid (DCA) and allocholic acid (ACA). Plays a essential role in BA homeostasis through the regulation of genes involved in BA synthesis, conjugation and enterohepatic circulation. Also regulates lipid and glucose homeostasis and is involved innate immune response (PubMed:10334992, PubMed:10334993, PubMed:21383957, PubMed:22820415). The FXR-RXR heterodimer binds predominantly to farnesoid X receptor response elements (FXREs) containing two inverted repeats of the consensus sequence 5'-AGGTCA-3' in which the monomers are spaced by 1 nucleotide (IR-1) but…
Heterodimer (via C-terminus) with RXRA (via DBD); the heterodimerization enhances the binding affinity for LXXLL motifs from coactivators (PubMed:23462506, PubMed:30275017). Binds DNA predominantly as a heterodimer with RXRA. After activation by agonist binding interacts with coactivators. Interacts with NCOA1, NCOA2, PPARGC1A, CARM1, SETD7, PRMT1, GPS2, SMARCA4 and MED1 (PubMed:12718892,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6HL1 | X-ray | 1.6 Å | A=258-486 |
| 6HL0 | X-ray | 1.66 Å | A=258-486 |
| 4OIV | X-ray | 1.7 Å | A/B=258-483 |
| 5Q0I | X-ray | 1.7 Å | A=258-486 |
| 1OSH | X-ray | 1.8 Å | A=257-486 |
| 5Q0K | X-ray | 1.8 Å | A=258-486 |
| 5Q0P | X-ray | 1.8 Å | A/C=258-486 |
| 5Q14 | X-ray | 1.85 Å | A/C=258-486 |
| 5Q1E | X-ray | 1.85 Å | A=258-486 |
| 5Q0V | X-ray | 1.87 Å | A/C=258-486 |
| 5Q1D | X-ray | 1.89 Å | A/C=258-486 |
| 3BEJ | X-ray | 1.9 Å | A/B=249-486 |
| 3L1B | X-ray | 1.9 Å | A=258-486 |
| 3OLF | X-ray | 1.9 Å | A/C=258-486 |
| 3OMK | X-ray | 1.9 Å | A/C=258-486 |
| 5Q0O | X-ray | 1.9 Å | A/C=258-486 |
| 5Q0U | X-ray | 1.9 Å | A/C=258-486 |
| 5Q0W | X-ray | 1.9 Å | A=258-486 |
| 5Q13 | X-ray | 1.9 Å | A/C=258-486 |
| 5Q15 | X-ray | 1.9 Å | A/C=258-486 |
Showing 20 of 89 experimental structures (best resolution first).
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