MolNFT v1 · #38727 · protein
Crystal structure of human tr alpha bound T3 in orthorhombic space group
2H79 · Thra protein: “Crystal structure of human tr alpha bound T3 in orthorhombic space group”. X-ray diffraction, 1 ligand (T3), 4 pockets (best druggability 0.83). MolNFT v1 #38727 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2H79
- Type
- protein
- Length
- 267 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 | 267 | 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 | 181 | 0.83 | 0.97 | 31 | T3 |
| 2 | 140 | 0.44 | 0.76 | 20 | empty |
| 3 | 115 | 0.40 | 0.76 | 18 | empty |
| 4 | 65 | 0.29 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 5 modified (artifact).
Compared structures
- 2H79 · Crystal Structure of human TR alpha bound T3 in orthorhombic 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 2H79 · PDBe 2H79 · UniProt Q6FH41
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