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Structure of tr-beta bound to selective thyromimetic gc-1
Analyse Structure of tr-beta bound to selective thyromimetic gc-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IMY
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thyroid hormone receptor beta
- UniProt
- P10828
- Ligands
- B72
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thyroid hormone receptor beta | protein | 251 | 67% helix, 4% strand | P10828 |
Ligands and binding sites
- B72 · {4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.83 | 0.97 | 32 | B72 |
| 2 | 127 | 0.43 | 0.77 | 20 | empty |
| 3 | 121 | 0.39 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 3 modified (artifact).
Compared structures
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 3IMY · PDBe 3IMY · UniProt P10828
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