Crystal structure of the human RXR alpha ligand binding domain bound to the synthetic agonist compound BMS 649 and a coactivator peptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 16 Oct 2002.
Explore 1MVC in 3D Show helices and sheets RCSB PDB PDBe
1MVC 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 | 264-285 | 22 | |
| α-helix | 289-291 | 3 | |
| α-helix | 294-316 | 23 | |
| β-strand | 323-325 | 3 | 1 |
| β-strand | 331-333 | 3 | 1 |
| α-helix | 334-339 | 6 | |
| 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 | 473-479 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RXR retinoid X receptor | A | protein | 240 | Homo sapiens | P19793 (AlphaFold model) |
| Nuclear receptor coactivator 2 | B | protein | 13 | Q15596 (AlphaFold model) |
>1MVC_1 RXR retinoid X receptor (chains A) TSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEW AKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGV GAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEA YCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
>1MVC_2 Nuclear receptor coactivator 2 (chains B) KHKILHRLLQDSS
| ID | Name | Formula | Copies |
|---|---|---|---|
| BM6 | 4-[2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydro-naphthalen-2-yl)-[1,3]DIOXOLAN-2-Y… | C24 H27 O4 | 1 |
Molecular Recognition of Agonist Ligands by RXRs. Egea, P.F., Mitschler, A., Moras, D. Mol Endocrinol (2002) 16:987-997. DOI 10.1210/me.16.5.987 · 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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