Human lxr beta hormone receptor complexed with T0901317. Determined by X-ray diffraction at 2.8 Å resolution. Released 9 Sept 2003.
Explore 1PQC in 3D Show helices and sheets RCSB PDB PDBe
1PQC contains 44 α-helices and 12 β-strands across 4 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 | 222-243 | 22 | |
| α-helix | 246-247 | 2 | |
| α-helix | 262-286 | 25 | |
| α-helix | 292-294 | 3 | |
| α-helix | 297-318 | 22 | |
| β-strand | 320-321 | 2 | 1 |
| β-strand | 326-330 | 5 | 1 |
| β-strand | 333-336 | 4 | 1 |
| α-helix | 337-342 | 6 | |
| α-helix | 347-363 | 17 | |
| α-helix | 367-378 | 12 | |
| α-helix | 389-410 | 22 | |
| α-helix | 417-443 | 27 | |
| α-helix | 448-450 | 3 | |
| α-helix | 451-457 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 222-238 | 17 | |
| α-helix | 240-244 | 5 | |
| α-helix | 262-288 | 27 | |
| α-helix | 292-294 | 3 | |
| α-helix | 297-318 | 22 | |
| β-strand | 320-321 | 2 | 2 |
| β-strand | 326-329 | 4 | 2 |
| β-strand | 333-336 | 4 | 2 |
| α-helix | 337-342 | 6 | |
| α-helix | 347-363 | 17 | |
| α-helix | 367-378 | 12 | |
| α-helix | 389-410 | 22 | |
| α-helix | 417-443 | 27 | |
| α-helix | 448-450 | 3 | |
| α-helix | 451-457 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 222-238 | 17 | |
| α-helix | 261-287 | 27 | |
| α-helix | 292-294 | 3 | |
| α-helix | 297-318 | 22 | |
| β-strand | 320-321 | 2 | 3 |
| β-strand | 326-330 | 5 | 3 |
| β-strand | 333-335 | 3 | 3 |
| α-helix | 337-342 | 6 | |
| α-helix | 347-363 | 17 | |
| α-helix | 367-378 | 12 | |
| α-helix | 389-410 | 22 | |
| α-helix | 417-443 | 27 | |
| α-helix | 451-457 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 222-241 | 20 | |
| α-helix | 261-288 | 28 | |
| α-helix | 292-294 | 3 | |
| α-helix | 297-318 | 22 | |
| β-strand | 320-321 | 2 | 4 |
| β-strand | 326-327 | 2 | 4 |
| β-strand | 335 | 1 | 4 |
| α-helix | 337-342 | 6 | |
| α-helix | 347-363 | 17 | |
| α-helix | 367-378 | 12 | |
| α-helix | 389-410 | 22 | |
| α-helix | 417-442 | 26 | |
| α-helix | 451-457 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Oxysterols receptor LXR-beta | A, B, C, D | protein | 253 | Homo sapiens | P55055 (AlphaFold model) |
>1PQC_1 Oxysterols receptor LXR-beta (chains A, B, C, D) GSHMGEGEGVQLTAAQELMIQQLVAAQLQCNKRSFSDQPKVTPWPLGADPQSRDARQQRF AHFTELAIISVQEIVDFAKQVPGFLQLGREDQIALLKASTIEIMLLETARRYNHETECIT FLKDFTYSKDDFHRAGLQVEFINPIFEFSRAMRRLGLDDAEYALLIAINIFSADRPNVQE PGRVEALQQPYVEALLSYTRIKRPQDQLRFPRMLMKLVSLRTLSSVHSEQVFALRLQDKK LPPLLSEIWDVHE
| ID | Name | Formula | Copies |
|---|---|---|---|
| 444 | N-(2,2,2-trifluoroethyl)-N-{4-[2,2,2-trifluoro-1-hydroxy-1-(trifluoromethyl)eth… | C17 H12 F9 N O3 S | 4 |
The three-dimensional structure of the liver X receptor beta reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands. Farnegardh, M., Bonn, T., Sun, S. et al. J Biol Chem (2003) 278:38821-38828. DOI 10.1074/jbc.M304842200 · PubMed
Other PDB entries of the same protein (UniProt P55055 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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