4ZSH: RXR LBD

RXR LBD in complex with 9-cis-13,14-dihydroretinoic acid. Determined by X-ray diffraction at 1.8 Å resolution. Released 30 Mar 2016.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
2
Atoms
1,981
Mol. weight
28.74 kDa
Ligands
4XW
Released
30 Mar 2016

Explore 4ZSH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZSH contains 13 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: 12 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix232-24211
α-helix264-28522
α-helix294-31623
β-strand323-32531
β-strand331-33331
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-helix449-4546
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix473-4797

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Retinoic acid receptor RXR-alphaAprotein240Homo sapiensP19793 (AlphaFold model)
NCoA2 peptideBprotein13Homo sapiensQ15596 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4ZSH_1 Retinoic acid receptor RXR-alpha (chains A)
TSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEW
AKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGV
GAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEA
YCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
Sequence of entity 2 (B), FASTA
>4ZSH_2 NCoA2 peptide (chains B)
KHKILHRLLQDSS

Ligands and cofactors

IDNameFormulaCopies
4XW(5S,6S,9R,13R)-2,3-didehydro-5,6,7,8,9,10,11,12,13,14-decahydroretinoic acidC20 H36 O21

Primary citation

9-cis-13,14-Dihydroretinoic Acid Is an Endogenous Retinoid Acting as RXR Ligand in Mice. Ruhl, R., Krzyzosiak, A., Niewiadomska-Cimicka, A. et al. PLoS Genet (2015) 11:e1005213-e1005213. DOI 10.1371/journal.pgen.1005213 · 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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