X-ray structure of human PPARalpha ligand binding domain-intrinsic fatty acid (E. coli origin)-PGC1alpha coactivator peptide co-crystals obtained by cross-seeding. Determined by X-ray diffraction at 1.59 Å resolution. Released 7 May 2025.
Explore 9IWN in 3D Show helices and sheets RCSB PDB PDBe
9IWN contains 19 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 | 203-217 | 15 | |
| α-helix | 222-230 | 9 | |
| α-helix | 237-238 | 2 | |
| β-strand | 239-241 | 3 | 1 |
| α-helix | 244-254 | 11 | |
| α-helix | 256-259 | 4 | |
| α-helix | 268-292 | 25 | |
| α-helix | 297-299 | 3 | |
| α-helix | 302-321 | 20 | |
| α-helix | 322-324 | 3 | |
| β-strand | 325-326 | 2 | 1 |
| β-strand | 329-332 | 4 | 1 |
| β-strand | 337-340 | 4 | 1 |
| α-helix | 341-346 | 6 | |
| α-helix | 348 | 1 | |
| α-helix | 351-353 | 3 | |
| α-helix | 356-366 | 11 | |
| α-helix | 372-383 | 12 | |
| α-helix | 394-415 | 22 | |
| α-helix | 422-450 | 29 | |
| α-helix | 455-457 | 3 | |
| α-helix | 458-464 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 689-695 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peroxisome proliferator-activated receptor alpha | A | protein | 273 | Homo sapiens | Q07869 (AlphaFold model) |
| Peroxisome proliferator-activated receptor gamma coactivator 1-alpha | B | protein | 15 | Homo sapiens | Q9UBK2 (AlphaFold model) |
>9IWN_1 Peroxisome proliferator-activated receptor alpha (chains A) GSHMTADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFVIHDMETLCMAEKTLV AKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYE AIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFDFAMKFNALELDDSDI SLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQ LVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY
>9IWN_2 Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (chains B) EAEEPSLLKKLLLAP
| ID | Name | Formula | Copies |
|---|---|---|---|
| PLM | Palmitic acid | C16 H32 O2 | 1 |
Water and common crystallization additives (GOL) are not listed.
Competitive Ligand-Induced Recruitment of Coactivators to Specific PPAR alpha / delta / gamma Ligand-Binding Domains Revealed by Dual-Emission FRET and X-Ray Diffraction of Cocrystals. Kamata, S., Honda, A., Yashiro, S. et al. Antioxidants (Basel) (2025) 14. DOI 10.3390/antiox14040494 · PubMed
Other PDB entries of the same protein (UniProt Q07869 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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