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

ElementResiduesLengthSheet
α-helix232-24110
α-helix243-2453
α-helix246-2505
α-helix264-28421
α-helix289-2913
α-helix294-31623
α-helix317-3193
β-strand324-32521
β-strand331-33221
α-helix334-3396
α-helix343-3486
α-helix349-3546
α-helix355-3606
α-helix364-37512
α-helix386-40722
α-helix414-4196
α-helix422-44221
α-helix449-4557
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix473-4808
Chain C: 13 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix1232-124211
α-helix1264-128522
α-helix1289-12913
α-helix1294-131623
β-strand1323-132532
β-strand1331-133332
α-helix1334-13396
α-helix1343-13486
α-helix1349-13546
α-helix1355-13595
α-helix1364-137512
α-helix1386-140722
α-helix1414-14196
α-helix1422-144221
α-helix1449-14546
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix1473-14808
Chain E: 16 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix2232-224110
α-helix2243-22453
α-helix2246-22527
α-helix2264-228421
α-helix2289-22913
α-helix2294-231623
α-helix2317-23193
β-strand2324-232523
β-strand2331-233223
α-helix2334-23396
α-helix2343-23486
α-helix2349-23546
α-helix2355-23606
α-helix2364-237512
α-helix2386-240722
α-helix2414-24196
α-helix2422-244221
α-helix2449-24557
Chain F: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2473-24808
Chain G: 12 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix3232-324211
α-helix3264-328522
α-helix3294-331623
β-strand3323-332534
β-strand3331-333334
α-helix3334-33407
α-helix3343-33486
α-helix3349-33546
α-helix3355-33595
α-helix3364-337512
α-helix3386-340722
α-helix3414-34196
α-helix3422-344221
α-helix3449-34557
Chain H: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix3473-34808

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RXR retinoid X receptorA, C, E, Gprotein240Homo sapiensP19793 (AlphaFold model)
Nuclear receptor coactivator 2B, D, F, Hprotein13synthetic constructQ15596 (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

IDNameFormulaCopies
BM64-[2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydro-naphthalen-2-yl)-[1,3]DIOXOLAN-2-Y…C24 H27 O44

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:

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