Research workbench
Crystal structure of transthyretin in complex with ligand C-7
Analyse Crystal structure of transthyretin in complex with ligand C-7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AC2
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin
- UniProt
- P02766
- Ligands
- 43F
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transthyretin | protein | 115 | 6% helix, 53% strand | P02766 |
Ligands and binding sites
- 43F · 2,4-dichloro-1-[4-(chloromethyl)-2-methoxyphenoxy]benzene · 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 | 64 | 0.33 | 0.76 | 16 | empty |
| 2 | 70 | 0.32 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 936 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 4AC2 · Crystal structure of transthyretin in complex with ligand C-7 · 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 P02766
- Elsewhere: RCSB PDB 4AC2 · PDBe 4AC2 · UniProt P02766
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.