Research workbench
Tr receptor mutations conferring hormone resistance and reduced corepressor release exhibit decreased stability in the nterminal lbd
Analyse Tr receptor mutations conferring hormone resistance and reduced corepressor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NQ0
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thyroid hormone receptor beta-1
- UniProt
- P10828
- Ligands
- 4HY, ARS
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thyroid hormone receptor beta-1 | protein | 253 | 67% helix, 4% strand | P10828 |
Ligands and binding sites
- 4HY · [4-(4-hydroxy-3-iodo-phenoxy)-3,5-diiodo-phenyl]-acetic acid · ligand · chains A
- ARS · Arsenic · metal · 6 copies · 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 | 199 | 0.82 | 0.96 | 31 | 4HY |
| 2 | 125 | 0.45 | 0.77 | 20 | empty |
| 3 | 109 | 0.37 | 0.74 | 16 | empty |
Compared structures
- 1NQ0 · TR Receptor Mutations Conferring Hormone Resistance and Reduced Corepressor Release… · 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 0.96
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 1NQ0 · PDBe 1NQ0 · UniProt P10828
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