Crystal structure of the ligand binding domain of the retinoid X receptor alpha in complex with 3-(2'-methoxy)-tetrahydronaphtyl cinnamic acid and a fragment of the coactivator TIF-2. Determined by X-ray diffraction at 1.8 Å resolution. Released 9 Oct 2007.
Explore 2P1T in 3D Show helices and sheets RCSB PDB PDBe
2P1T contains 14 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 | 232-242 | 11 | |
| 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 | 334-338 | 5 | |
| α-helix | 343-348 | 6 | |
| α-helix | 349-354 | 6 | |
| α-helix | 355-359 | 5 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 688-695 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoic acid receptor RXR-alpha | A | protein | 240 | Homo sapiens | P19793 (AlphaFold model) |
| Nuclear receptor coactivator 2 peptide | B | protein | 13 | Q15596 (AlphaFold model) |
>2P1T_1 Retinoic acid receptor RXR-alpha (chains A) TSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEW AKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGV GAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEA YCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
>2P1T_2 Nuclear receptor coactivator 2 peptide (chains B) KHKILHRLLQDSS
| ID | Name | Formula | Copies |
|---|---|---|---|
| 3TN | (2E)-3-[4-hydroxy-3-(3-methoxy-5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen… | C24 H28 O4 | 1 |
Modulators of the structural dynamics of the retinoid X receptor to reveal receptor function. Nahoum, V., Perez, E., Germain, P. et al. Proc Natl Acad Sci U S A (2007) 104:17323-17328. DOI 10.1073/pnas.0705356104 · 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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