MolNFT v2 · #6300 · protein
Transthyretin THR119MET protein stabilisation
1F86 · Transthyretin THR119MET variant: “Transthyretin THR119MET protein stabilisation”. X-ray diffraction at 1.1, 1 ligand (T44), 2 pockets (best druggability 0.33). MolNFT v2 #6300 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1F86
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.1
- Source
- Homo sapiens
- Molecule
- Transthyretin THR119MET variant
- UniProt
- P02766
- Ligands
- T44
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · resolution 1.1 · 1 distinct chain · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transthyretin THR119MET variant | protein | 115 | 6% helix, 53% strand | P02766 |
Ligands and binding sites
- T44 · 3,5,3',5'-tetraiodo-L-thyronine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.33 | 0.75 | 15 | empty |
| 2 | 55 | 0.32 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 933 Ų buried · 17 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 P02766
- Elsewhere: RCSB PDB 1F86 · PDBe 1F86 · UniProt P02766
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