MolNFT v1 · #50958 · protein
Tertiary structures of three amyloidogenic transthyretin variants and implications for amyloid fibril formation
2TRH: “Tertiary structures of three amyloidogenic transthyretin variants and implications for amyloid fibril…”. X-ray diffraction, 3 pockets (best druggability 0.30). MolNFT v1 #50958 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2TRH
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin
- UniProt
- P02766
- Pockets
- 3 · best druggability 0.30
Structure
x-ray diffraction · 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 B against B, 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
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