Research workbench
Structure and specificity of nuclear receptor-coactivator interactions
Analyse Structure and specificity of nuclear receptor-coactivator interactions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BSX
- Type
- protein
- Length
- 510 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (thyroid hormone receptor beta); Protein (GRIP1)
- UniProt
- P10828
- Ligands
- T3
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (thyroid hormone receptor beta) | protein | 243 | 63% helix, 4% strand | P10828 |
| X, Y | Protein (GRIP1) | protein | 12 | 58% helix, 0% strand | — |
Ligands and binding sites
- T3 · 3,5,3'triiodothyronine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.84 | 0.96 | 31 | T3 |
| 2 | 222 | 0.84 | 0.96 | 31 | T3 |
| 3 | 136 | 0.45 | 0.77 | 23 | empty |
| 4 | 110 | 0.43 | 0.78 | 22 | empty |
| 5 | 102 | 0.38 | 0.75 | 17 | empty |
Interfaces
2 interfaces between chains.
- B–Y · 440 Ų buried · 5 hydrogen bonds · protein-protein
- A–X · 435 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1BSX · Structure and specificity of nuclear receptor-coactivator interactions · the same entry in another collection · chain A against A, TM-score 1.00
- P10828 · AlphaFold monomer V2.0 prediction for thyroid hormone receptor beta (P10828) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P10828
- Elsewhere: RCSB PDB 1BSX · PDBe 1BSX · UniProt P10828
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