Research workbench
Crystal structure of human retinoic X receptor alpha ligand-binding domain complexed with LX0278 and SRC1 peptide
Analyse Crystal structure of human retinoic X receptor alpha ligand-binding domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PCU
- Type
- protein
- Length
- 221 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoic acid receptor rxr-alpha; Nuclear receptor coactivator 2
- UniProt
- P19793, Q15596
- Ligands
- LX8
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoic acid receptor rxr-alpha | protein | 211 | 69% helix, 3% strand | P19793 |
| B | Nuclear receptor coactivator 2 | protein | 10 | 80% helix, 0% strand | Q15596 |
Ligands and binding sites
- LX8 · 2-[(2S)-6-(2-methylbut-3-en-2-yl)-7-oxo-2,3-dihydro-7H-furo[3,2-g]chromen-2-yl]propan-2-yl acetate · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 287 | 0.83 | 0.93 | 39 | LX8 |
| 2 | 88 | 0.33 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 569 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3PCU · Crystal structure of human retinoic X receptor alpha ligand-binding domain complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P19793
- Every structure of UniProt Q15596
- Elsewhere: RCSB PDB 3PCU · PDBe 3PCU · UniProt P19793 · UniProt Q15596
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