Q96RI1: Bile acid receptor (NR1H4)

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.

Gene
NR1H4
Organism
Homo sapiens
Length
486 residues
Mean pLDDT
68.8
Model
AF-Q96RI1-F1 v6
Model created
1 Aug 2025
PDB structures
89

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate36%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions33%

What pLDDT means and how to read it

Function

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…

Subunit structure

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,…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6HL1X-ray1.6 ÅA=258-486
6HL0X-ray1.66 ÅA=258-486
4OIVX-ray1.7 ÅA/B=258-483
5Q0IX-ray1.7 ÅA=258-486
1OSHX-ray1.8 ÅA=257-486
5Q0KX-ray1.8 ÅA=258-486
5Q0PX-ray1.8 ÅA/C=258-486
5Q14X-ray1.85 ÅA/C=258-486
5Q1EX-ray1.85 ÅA=258-486
5Q0VX-ray1.87 ÅA/C=258-486
5Q1DX-ray1.89 ÅA/C=258-486
3BEJX-ray1.9 ÅA/B=249-486
3L1BX-ray1.9 ÅA=258-486
3OLFX-ray1.9 ÅA/C=258-486
3OMKX-ray1.9 ÅA/C=258-486
5Q0OX-ray1.9 ÅA/C=258-486
5Q0UX-ray1.9 ÅA/C=258-486
5Q0WX-ray1.9 ÅA=258-486
5Q13X-ray1.9 ÅA/C=258-486
5Q15X-ray1.9 ÅA/C=258-486

Showing 20 of 89 experimental structures (best resolution first).

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