Research workbench
Nvgsnty segment from islet amyloid polypeptide (iapp or amylin), dehydrated crystal form
Analyse Nvgsnty segment from islet amyloid polypeptide (iapp or amylin), dehydrated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FTL
- Type
- protein
- Length
- 14 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nvgsnty heptapeptide segment from islet amyloid polypeptide
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nvgsnty heptapeptide segment from islet amyloid polypeptide | protein | 7 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 145 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3FTL · NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), dehydrated crystal form · 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 3FTL · PDBe 3FTL
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