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Crystal structure of the human rxr alpha ligand binding domain bound to the eicosanoid dha (docosa hexaenoic acid) and a coactivator peptide

Analyse Crystal structure of the human rxr alpha ligand binding domain bound to the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MV9
Type
protein
Length
225 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rxr retinoid X receptor; Nuclear receptor coactivator 2
UniProt
P19793, Q15596
Ligands
HXA
Pockets
2 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARxr retinoid X receptorprotein21470% helix, 3% strandP19793
BNuclear receptor coactivator 2protein1173% helix, 0% strandQ15596

Ligands and binding sites

  • HXA · Docosa-4,7,10,13,16,19-hexaenoic acid · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13300.840.9340HXA
21940.460.7431empty

Interfaces

1 interface between chains.

  • A–B · 622 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 1MV9 · Crystal Structure of the human RXR alpha ligand binding domain bound to the eicosanoid… · the same entry in another collection · chain A against A, TM-score 1.00

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