Research workbench
Crystal structure of E61K mutated transthyretin
Analyse Crystal structure of E61K mutated transthyretin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KGB
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.3
- Source
- Homo sapiens
- Molecule
- Transthyretin
- UniProt
- P02766
- Ligands
- CA
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · resolution 1.3 · 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
- CA · Calcium ion · metal · chains A
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 | 73 | 0.34 | 0.75 | 15 | empty |
| 2 | 60 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 914 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6KGB · Crystal structure of E61K mutated transthyretin · 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 6KGB · PDBe 6KGB · UniProt P02766
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