Research workbench
Transthyretin-V/122/I cardiomyopathic mutant
Analyse Transthyretin-V/122/I cardiomyopathic mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TTR
- Type
- protein
- Length
- 233 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin
- UniProt
- P02766
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transthyretin | protein | 116 | 6% helix, 53% strand | P02766 |
| B | Transthyretin | protein | 117 | 6% helix, 50% strand | P02766 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.31 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 907 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 1TTR · Transthyretin-V/122/I cardiomyopathic mutant · 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 1TTR · PDBe 1TTR · UniProt P02766
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