Revealing a marine natural product as a novel agonist for retinoic acid receptors with a unique binding mode and antitumor activity. Determined by X-ray diffraction at 2.75 Å resolution. Released 3 Oct 2012.
Explore 4DQM in 3D Show helices and sheets RCSB PDB PDBe
4DQM contains 31 α-helices and 10 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 | 183-198 | 16 | |
| α-helix | 202-204 | 3 | |
| β-strand | 208 | 1 | 1 |
| α-helix | 222-244 | 23 | |
| α-helix | 249-251 | 3 | |
| α-helix | 254-274 | 21 | |
| β-strand | 277-278 | 2 | 2 |
| β-strand | 283-285 | 3 | 2 |
| β-strand | 290 | 1 | 1 |
| β-strand | 291-293 | 3 | 2 |
| α-helix | 294-297 | 4 | |
| α-helix | 298-302 | 5 | |
| α-helix | 303-305 | 3 | |
| α-helix | 306-316 | 11 | |
| α-helix | 317-319 | 3 | |
| α-helix | 323-334 | 12 | |
| α-helix | 345-366 | 22 | |
| α-helix | 373-378 | 6 | |
| α-helix | 380-389 | 10 | |
| α-helix | 391-401 | 11 | |
| α-helix | 408-414 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1434-1440 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 183-198 | 16 | |
| α-helix | 202-204 | 3 | |
| β-strand | 208 | 1 | 3 |
| α-helix | 222-244 | 23 | |
| α-helix | 249-251 | 3 | |
| α-helix | 254-274 | 21 | |
| β-strand | 277 | 1 | 4 |
| β-strand | 284-285 | 2 | 4 |
| β-strand | 290 | 1 | 3 |
| β-strand | 291-292 | 2 | 4 |
| α-helix | 294-297 | 4 | |
| α-helix | 298-302 | 5 | |
| α-helix | 305-315 | 11 | |
| α-helix | 323-334 | 12 | |
| α-helix | 345-366 | 22 | |
| α-helix | 373-389 | 17 | |
| α-helix | 391-399 | 9 | |
| α-helix | 408-414 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1436-1439 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoic acid receptor alpha | A, C | protein | 234 | Homo sapiens | P10276 (AlphaFold model) |
| Nuclear receptor coactivator 1 | B, D | protein | 10 | Homo sapiens | Q15788 (AlphaFold model) |
>4DQM_1 Retinoic acid receptor alpha (chains A, C) PEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVE FAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAG FGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDRVDMLQEPLLEALKV YVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLE
>4DQM_2 Nuclear receptor coactivator 1 (chains B, D) KSLLQQLLTE
| ID | Name | Formula | Copies |
|---|---|---|---|
| LUF | (5S)-4-[(3E,7E)-4,8-dimethyl-10-(2,6,6-trimethylcyclohex-1-en-1-yl)deca-3,7-die… | C25 H38 O3 | 2 |
Revealing a natural marine product as a novel agonist for retinoic acid receptors with a unique binding mode and inhibitory effects on cancer cells. Wang, S., Wang, Z., Lin, S. et al. Biochem J (2012) 446:79-87. DOI 10.1042/BJ20120726 · PubMed
Other PDB entries of the same protein (UniProt P10276 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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