Research workbench
Tr variant D355R
Analyse Tr variant D355R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D57
- Type
- protein
- Length
- 493 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thyroid hormone receptor beta
- UniProt
- P10828
- Ligands
- 4HY, SO4
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thyroid hormone receptor beta | protein | 245 | 66% helix, 5% strand | P10828 |
| B | Thyroid hormone receptor beta | protein | 248 | 66% helix, 4% strand | P10828 |
Ligands and binding sites
- 4HY · [4-(4-hydroxy-3-iodo-phenoxy)-3,5-diiodo-phenyl]-acetic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.84 | 0.97 | 30 | 4HY |
| 2 | 190 | 0.84 | 0.98 | 28 | 4HY |
| 3 | 401 | 0.66 | 0.80 | 31 | empty |
| 4 | 426 | 0.65 | 0.78 | 36 | empty |
| 5 | 57 | 0.36 | 0.78 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 722 Ų buried · 9 hydrogen bonds · protein-protein
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 3D57 · PDBe 3D57 · UniProt P10828
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