MolNFT v1 · #31630 · protein
The crystal structure of 2,4-dinitrophenol in complex with the amyloidogenic variant transthyretin TYR78PHE
2B16: “The crystal structure of 2,4-dinitrophenol in complex with the amyloidogenic variant transthyretin TYR78PHE”. X-ray diffraction, 1 ligand (DNF), 2 pockets (best druggability 0.34). MolNFT v1 #31630 on GenesisL1: 3D structure…
- PDB
- 2B16
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin
- UniProt
- P02766
- Ligands
- DNF
- Pockets
- 2 · best druggability 0.34
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
- DNF · 2,4-dinitrophenol · 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 | 65 | 0.34 | 0.76 | 17 | empty |
| 2 | 51 | 0.29 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 893 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2B16 · The crystal structure of 2,4-dinitrophenol in complex with the amyloidogenic variant… · 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 2B16 · PDBe 2B16 · UniProt P02766
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