1MZN: RXR retinoid X receptor
Crystal structure at 1.9 angstroems resolution of the homodimer of 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 23 Oct 2002.
- Method
- X-ray diffraction
- Resolution
- 1.9 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 8
- Atoms
- 8,177
- Mol. weight
- 115.26 kDa
- Ligands
- BM6
- Released
- 23 Oct 2002
Explore 1MZN in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1MZN contains 61 α-helices and 8 β-strands across 8 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.
Chain A: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 232-241 | 10 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-250 | 5 | |
| α-helix | 264-284 | 21 | |
| α-helix | 289-291 | 3 | |
| α-helix | 294-316 | 23 | |
| α-helix | 317-319 | 3 | |
| β-strand | 324-325 | 2 | 1 |
| β-strand | 331-332 | 2 | 1 |
| α-helix | 334-339 | 6 | |
| α-helix | 343-348 | 6 | |
| α-helix | 349-354 | 6 | |
| α-helix | 355-360 | 6 | |
| α-helix | 364-375 | 12 | |
| α-helix | 386-407 | 22 | |
| α-helix | 414-419 | 6 | |
| α-helix | 422-442 | 21 | |
| α-helix | 449-455 | 7 | |
Chain B: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 473-480 | 8 | |
Chain C: 13 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1232-1242 | 11 | |
| α-helix | 1264-1285 | 22 | |
| α-helix | 1289-1291 | 3 | |
| α-helix | 1294-1316 | 23 | |
| β-strand | 1323-1325 | 3 | 2 |
| β-strand | 1331-1333 | 3 | 2 |
| α-helix | 1334-1339 | 6 | |
| α-helix | 1343-1348 | 6 | |
| α-helix | 1349-1354 | 6 | |
| α-helix | 1355-1359 | 5 | |
| α-helix | 1364-1375 | 12 | |
| α-helix | 1386-1407 | 22 | |
| α-helix | 1414-1419 | 6 | |
| α-helix | 1422-1442 | 21 | |
| α-helix | 1449-1454 | 6 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1473-1480 | 8 | |
Chain E: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2232-2241 | 10 | |
| α-helix | 2243-2245 | 3 | |
| α-helix | 2246-2252 | 7 | |
| α-helix | 2264-2284 | 21 | |
| α-helix | 2289-2291 | 3 | |
| α-helix | 2294-2316 | 23 | |
| α-helix | 2317-2319 | 3 | |
| β-strand | 2324-2325 | 2 | 3 |
| β-strand | 2331-2332 | 2 | 3 |
| α-helix | 2334-2339 | 6 | |
| α-helix | 2343-2348 | 6 | |
| α-helix | 2349-2354 | 6 | |
| α-helix | 2355-2360 | 6 | |
| α-helix | 2364-2375 | 12 | |
| α-helix | 2386-2407 | 22 | |
| α-helix | 2414-2419 | 6 | |
| α-helix | 2422-2442 | 21 | |
| α-helix | 2449-2455 | 7 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2473-2480 | 8 | |
Chain G: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3232-3242 | 11 | |
| α-helix | 3264-3285 | 22 | |
| α-helix | 3294-3316 | 23 | |
| β-strand | 3323-3325 | 3 | 4 |
| β-strand | 3331-3333 | 3 | 4 |
| α-helix | 3334-3340 | 7 | |
| α-helix | 3343-3348 | 6 | |
| α-helix | 3349-3354 | 6 | |
| α-helix | 3355-3359 | 5 | |
| α-helix | 3364-3375 | 12 | |
| α-helix | 3386-3407 | 22 | |
| α-helix | 3414-3419 | 6 | |
| α-helix | 3422-3442 | 21 | |
| α-helix | 3449-3455 | 7 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3473-3480 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| RXR retinoid X receptor | A, C, E, G | protein | 240 | Homo sapiens | P19793 (AlphaFold model) |
| Nuclear receptor coactivator 2 | B, D, F, H | protein | 13 | synthetic construct | Q15596 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>1MZN_1 RXR retinoid X receptor (chains A, C, E, G)
TSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEW
AKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGV
GAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEA
YCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
Sequence of entity 2 (B, D, F, H), FASTA
>1MZN_2 Nuclear receptor coactivator 2 (chains B, D, F, H)
KHKILHRLLQDSS
Ligands and cofactors
| 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 | 4 |
Primary citation
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:
- 9QX6 1.46 Å, Crystal structure of RXR alpha LBD bound to a synthetic agonist FN537 and a coactivator…
- 6LB4 1.5 Å, Crystal structure of dimeric RXR-LBD complexed with NEt-3ME and TIF2 co-activator
- 7A77 1.5 Å, Crystal structure of RXR alpha LBD in complexes with palmitic acid and GRIP-1 peptide
- 6FBQ 1.6 Å, Crystal Structure of the Human Retinoid X Receptor DNA-Binding Domain Bound to the Human…
- 9RMR 1.65 Å, Crystal structure of RXR alpha LBD bound to a synthetic agonist FN558 and a coactivator…
- 1DSZ 1.7 Å, Structure of the rxr/rar DNA-binding domain heterodimer in complex with the retinoic…
- 5MKU 1.78 Å, Crystal structure of the Retinoid X Receptor alpha in complex with synthetic honokiol…
- 2P1T 1.8 Å, Crystal structure of the ligand binding domain of the retinoid X receptor alpha in…
- 4ZSH 1.8 Å, RXR LBD in complex with 9-cis-13,14-dihydroretinoic acid
- 6L6K 1.8 Å, Crystal structure of dimeric RXRalpha-LBD complexed with partial agonist CBt-PMN and SRC1
- 7UW2 1.88 Å, Crystal structure of human Retinoid X receptor alpha ligand binding domain complex with…
- 6STI 1.89 Å, Crystal structure of RXRalpha LBD in complex with LG 100754 and a coactivator peptide
Browse structure collections
About this viewer
MolViewer shows 1MZN directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.