1MVC: Human RXR alpha ligand binding domain

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.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
2
Atoms
1,988
Mol. weight
28.82 kDa
Ligands
BM6
Released
16 Oct 2002

Explore 1MVC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 13 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix232-24211
α-helix264-28522
α-helix289-2913
α-helix294-31623
β-strand323-32531
β-strand331-33331
α-helix334-3396
α-helix343-3486
α-helix349-3546
α-helix355-3595
α-helix364-37512
α-helix386-40722
α-helix414-4196
α-helix422-44221
α-helix449-4546
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix473-4797

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RXR retinoid X receptorAprotein240Homo sapiensP19793 (AlphaFold model)
Nuclear receptor coactivator 2Bprotein13Q15596 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1MVC_1 RXR retinoid X receptor (chains A)
TSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEW
AKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGV
GAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEA
YCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
Sequence of entity 2 (B), FASTA
>1MVC_2 Nuclear receptor coactivator 2 (chains B)
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 O41

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:

Browse structure collections

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