Research workbench
Tertiary structures of three amyloidogenic transthyretin variants and implications for amyloid fibril formation
Analyse Tertiary structures of three amyloidogenic transthyretin variants and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2TRH
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Homo sapiens
- Molecule
- Transthyretin
- UniProt
- P02766
- Pockets
- 3 · best druggability 0.30
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transthyretin | protein | 127 | 5% helix, 48% strand | P02766 |
Pockets
3 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 | 0.30 | 0.74 | 17 | empty |
| 2 | 61 | 0.30 | 0.75 | 14 | empty |
| 3 | 54 | 0.29 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 920 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 2TRH · Tertiary structures of three amyloidogenic transthyretin variants and implications for… · 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 2TRH · PDBe 2TRH · UniProt P02766
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.