Research workbench
Structure of the amyloid forming peptide vavhvf from transthyretin
Analyse Structure of the amyloid forming peptide vavhvf from transthyretin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C88
- Type
- protein
- Length
- 12 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.851
- Molecule
- Val-ala-val-his-val-phe
Structure
x-ray diffraction · resolution 1.851 · 1 distinct chain · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Val-ala-val-his-val-phe | protein | 6 | 0% helix, 50% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 269 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6C88 · Structure of the amyloid forming peptide vavhvf from 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
- Elsewhere: RCSB PDB 6C88 · PDBe 6C88
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