Research workbench
Crystal structure of the human rxr alpha ligand binding domain bound to the synthetic agonist compound bms 649 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
- 1MVC
- Type
- protein
- Length
- 223 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
- BM6
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rxr retinoid X receptor | protein | 212 | 70% helix, 3% strand | P19793 |
| B | Nuclear receptor coactivator 2 | protein | 11 | 64% helix, 0% strand | Q15596 |
Ligands and binding sites
- BM6 · 4-[2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydro-naphthalen-2-yl)-[1,3]dioxolan-2-yl]-benzoic 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.83 | 0.93 | 40 | BM6 |
| 2 | 102 | 0.39 | 0.75 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 613 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1MVC · Crystal structure of the human RXR alpha ligand binding domain bound to the synthetic… · 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 1MVC · PDBe 1MVC · UniProt P19793 · UniProt Q15596
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