MolNFT v2 · #50966 · 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 at 1.9. MolNFT v2 #50966 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- P02766
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 127 | — | P02766 |
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
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