Crystal structure of RXR alpha LBD bound to a synthetic agonist FN537 and a coactivator fragment. Determined by X-ray diffraction at 1.46 Å resolution. Released 13 Aug 2025.
Explore 9QX6 in 3D Show helices and sheets RCSB PDB PDBe
9QX6 contains 15 α-helices and 2 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 232-241 | 10 | |
| α-helix | 264-284 | 21 | |
| α-helix | 289-291 | 3 | |
| α-helix | 294-316 | 23 | |
| β-strand | 323-325 | 3 | 1 |
| β-strand | 331-333 | 3 | 1 |
| α-helix | 334-339 | 6 | |
| α-helix | 343-348 | 6 | |
| α-helix | 349-354 | 6 | |
| α-helix | 355-360 | 6 | |
| α-helix | 364-375 | 12 | |
| α-helix | 386-407 | 22 | |
| α-helix | 414-419 | 6 | |
| α-helix | 422-442 | 21 | |
| α-helix | 449-454 | 6 | |
| α-helix | 457-458 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 473-478 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoic acid receptor RXR-alpha | A | protein | 235 | Homo sapiens | P19793 (AlphaFold model) |
| Nuclear receptor coactivator 2 | B | protein | 10 | Homo sapiens | Q15596 (AlphaFold model) |
>9QX6_1 Retinoic acid receptor RXR-alpha (chains A) SDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIP HFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFD RVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHK YPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
>9QX6_2 Nuclear receptor coactivator 2 (chains B) HKILHRLLQD
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1JHO | 6S,6aS,7R,10S,10aR)-6-(3,5-bis(trifluoromethyl)phenyl)-5,6,6a,7,8,9,10,10a-octa… | C23 H19 F6 N O2 | 1 |
| A1JAT | (6R,6aR,7S,10R,10aS)-6-(3,5-bis(trifluoromethyl)phenyl)-5,6,6a,7,8,9,10,10a-oct… | C23 H19 F6 N O2 | 1 |
Development of an RXR Agonist Scaffold with Pronounced Homodimer Preference. Nawa, F., Kardanov, A., Kasch, T. et al. J Med Chem (2025) 68:16172-16187. DOI 10.1021/acs.jmedchem.5c01090 · PubMed
Other PDB entries of the same protein (UniProt P19793 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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