Oxysterols receptor LXR-beta (NR1H2) is a 460-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P55055.
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The mean pLDDT of this model is 80.3 (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 | 60% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 22% |
What pLDDT means and how to read it
Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into…
Forms a heterodimer with RXR. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner (PubMed:25661920). Interacts (when sumoylated) with GPS2; interaction with GPS2 onto hepatic acute phase protein promoters prevents N-Cor corepressor complex dissociation (PubMed:20159957). Interacts with ABCA12 and ABCA1; this interaction is required for ABCA1 localization to the cell surface and…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6S5K | X-ray | 1.6 Å | A=216-460 |
| 6S4N | X-ray | 1.9 Å | A/B/C/D=216-460 |
| 6S4T | X-ray | 2.0 Å | A=216-460 |
| 4RAK | X-ray | 2.04 Å | A/B=213-460 |
| 1PQ9 | X-ray | 2.1 Å | A/B/C/D=212-460 |
| 1UPV | X-ray | 2.1 Å | A=203-460 |
| 3L0E | X-ray | 2.3 Å | A=212-460 |
| 1PQ6 | X-ray | 2.4 Å | A/B/C/D=212-460 |
| 1UPW | X-ray | 2.4 Å | A=203-460 |
| 3KFC | X-ray | 2.4 Å | A/B/C/D=212-460 |
| 5JY3 | X-ray | 2.4 Å | A/B/C/D=213-460 |
| 4DK7 | X-ray | 2.45 Å | A/C=218-460 |
| 6K9H | X-ray | 2.5 Å | A/B=214-460 |
| 5HJP | X-ray | 2.6 Å | B/D=216-460 |
| 5KYA | X-ray | 2.6 Å | A/E=209-460 |
| 6JIO | X-ray | 2.6 Å | A/B/C/D=214-460 |
| 5I4V | X-ray | 2.61 Å | A/E=210-460 |
| 4DK8 | X-ray | 2.75 Å | A/C=218-460 |
| 1P8D | X-ray | 2.8 Å | A/B=213-460 |
| 1PQC | X-ray | 2.8 Å | A/B/C/D=212-460 |
Showing 20 of 25 experimental structures (best resolution first).
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