MolNFT v1 · #172106 · protein
Amyloid structure of amylin (iapp - islet amyloid polypeptide)
6ZRF: “Amyloid structure of amylin (iapp - islet amyloid polypeptide)”. Electron microscopy. MolNFT v1 #172106 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ZRF
- Type
- protein
- Length
- 300 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Islet amyloid polypeptide
- UniProt
- P10997
Structure
electron microscopy · 1 distinct chain · 0% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, B, D, F, H, J, L | Islet amyloid polypeptide | protein | 25 | 0% helix, 24% strand | P10997 |
Interfaces
30 interfaces between chains.
- H–J · 971 Ų buried · 33 hydrogen bonds · protein-protein
- B–D · 938 Ų buried · 28 hydrogen bonds · protein-protein
- C–E · 934 Ų buried · 28 hydrogen bonds · protein-protein
- F–H · 932 Ų buried · 29 hydrogen bonds · protein-protein
- D–F · 932 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (nonstandard).
Compared structures
- 6ZRF · amyloid structure of amylin (IAPP - islet amyloid polypeptide) · the same entry in another collection · chain L against L, 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 6ZRF · PDBe 6ZRF · UniProt P10997
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