Research workbench
Amyloid fibril structure of islet amyloid polypeptide
Analyse Amyloid fibril structure of 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
- 6Y1A
- Type
- protein
- Length
- 400 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Islet amyloid polypeptide
- UniProt
- P10997
- Ligands
- NH2
Structure
electron microscopy · 1 distinct chain · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Islet amyloid polypeptide | protein | 25 | 0% helix, 52% strand | P10997 |
Ligands and binding sites
- NH2 · Amino group · ion · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
41 interfaces between chains.
- H–J · 1056 Ų buried · 30 hydrogen bonds · protein-protein
- K–M · 1053 Ų buried · 30 hydrogen bonds · protein-protein
- C–E · 1053 Ų buried · 30 hydrogen bonds · protein-protein
- G–I · 1051 Ų buried · 29 hydrogen bonds · protein-protein
- D–F · 1051 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 6Y1A · Amyloid fibril structure of islet amyloid polypeptide · the same entry in another collection · chain P against P, 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 P10997
- Elsewhere: RCSB PDB 6Y1A · PDBe 6Y1A · UniProt P10997
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