Research workbench
Crystal structure of human tr alpha bound T3 in monoclinic space group
Analyse Crystal structure of human tr alpha bound T3 in monoclinic space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H77
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thra protein
- UniProt
- Q6FH41
- Ligands
- T3
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thra protein | protein | 255 | 63% helix, 5% strand | Q6FH41 |
Ligands and binding sites
- T3 · 3,5,3'triiodothyronine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.83 | 0.97 | 31 | T3 |
| 2 | 124 | 0.42 | 0.76 | 19 | empty |
| 3 | 69 | 0.32 | 0.75 | 18 | empty |
| 4 | 56 | 0.31 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 4 modified (artifact).
Compared structures
- 2H77 · Crystal structure of human TR alpha bound T3 in monoclinic space group · 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 Q6FH41
- Elsewhere: RCSB PDB 2H77 · PDBe 2H77 · UniProt Q6FH41
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