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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ailsst hexapeptide segment from islet amyloid polypeptide
Structure
x-ray diffraction · 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 D against D, 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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