Characterization of ligands for the orphan nuclear receptor RORbeta. Determined by X-ray diffraction at 1.5 Å resolution. Released 23 Sept 2003.
Explore 1NQ7 in 3D Show helices and sheets RCSB PDB PDBe
1NQ7 contains 18 α-helices and 4 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 | 209-226 | 18 | |
| α-helix | 231-237 | 7 | |
| α-helix | 240 | 1 | |
| β-strand | 241 | 1 | 1 |
| α-helix | 242-243 | 2 | |
| α-helix | 244-252 | 9 | |
| α-helix | 255-278 | 24 | |
| α-helix | 281-284 | 4 | |
| α-helix | 288-307 | 20 | |
| α-helix | 308-310 | 3 | |
| β-strand | 311-312 | 2 | 1 |
| β-strand | 317-320 | 4 | 1 |
| β-strand | 323-326 | 4 | 1 |
| α-helix | 327-333 | 7 | |
| α-helix | 336-350 | 15 | |
| α-helix | 356-367 | 12 | |
| α-helix | 378-399 | 22 | |
| α-helix | 405-411 | 7 | |
| α-helix | 413-433 | 21 | |
| α-helix | 435-440 | 6 | |
| α-helix | 444-450 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 688-695 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear receptor ror-beta | A | protein | 244 | Rattus norvegicus | P45446 (AlphaFold model) |
| Steroid receptor coactivator-1 | B | protein | 10 | Q15788 (AlphaFold model) |
>1NQ7_1 NUCLEAR RECEPTOR ROR-BETA (chains A) TMSEIDRIAQNIIKSHLETCQYTMEELHQLAWQTHTYEEIKAYQSKSREALWQQCAIQIT HAIQYVVEFAKRITGFMELCQNDQILLLKSGCLEVVLVRMCRAFNPLNNTVLFEGKYGGM QMFKALGSDDLVNEAFDFAKNLCSLQLTEEEIALFSSAVLISPDRAWLLEPRKVQKLQEK IYFALQHVIQKNHLDDETLAKLIAKIPTITAVCNLHGEKLQVFKQSHPDIVNTLFPPLYK ELFN
>1NQ7_2 STEROID RECEPTOR COACTIVATOR-1 (chains B) HKILHRLLQE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ARL | 7-(3,5-ditert-butylphenyl)-3-methylocta-2,4,6-trienoic acid | C23 H32 O2 | 1 |
All-trans retinoic acid is a ligand for the orphan nuclear receptor RORbeta. Stehlin-Gaon, C., Willmann, D., Zeyer, D. et al. Nat Struct Biol (2003) 10:820-825. DOI 10.1038/nsb979 · PubMed
Other PDB entries of the same protein (UniProt P45446 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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