Research workbench
AILSST segment from Islet Amyloid Polypeptide
Analyse AILSST segment from Islet Amyloid Polypeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FOD
- Type
- protein
- Length
- 48 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.4
- Molecule
- AILSST hexapeptide segment from Islet Amyloid Polypeptide
Structure
x-ray diffraction · resolution 1.4 · 1 distinct chain · 0% helix, 67% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | AILSST hexapeptide segment from Islet Amyloid Polypeptide | protein | 6 | 0% helix, 67% strand | — |
Interfaces
16 interfaces between chains.
- G–H · 244 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 244 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 240 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 238 Ų buried · 8 hydrogen bonds · protein-protein
- C–H · 116 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3FOD · Ailsst segment from islet amyloid polypeptide · 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 3FOD · PDBe 3FOD
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