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Cryo-EM structure of human islet amyloid polypeptide (hiapp, or amylin) fibrils

Analyse Cryo-EM structure of human islet amyloid polypeptide (hiapp, or amylin) fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VW2
Type
protein
Length
240 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Islet amyloid polypeptide (sumo-tagged)
UniProt
Q12306, P10997
Pockets
2 · best druggability 0.65

Structure

electron microscopy · 1 distinct chain · 0% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, JIslet amyloid polypeptide (sumo-tagged)protein240% helix, 46% strandQ12306, P10997

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1800.650.9225empty
2810.590.8825empty

Interfaces

17 interfaces between chains.

  • E–I · 939 Ų buried · 33 hydrogen bonds · protein-protein
  • A–E · 938 Ų buried · 33 hydrogen bonds · protein-protein
  • D–H · 938 Ų buried · 33 hydrogen bonds · protein-protein
  • B–F · 937 Ų buried · 33 hydrogen bonds · protein-protein
  • A–D · 936 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

  • 6VW2 · Cryo-EM structure of human islet amyloid polypeptide (hIAPP, or amylin) fibrils · the same entry in another collection · chain J against J, TM-score 1.00
  • P10997 · AlphaFold monomer V2.0 prediction for islet amyloid polypeptide (P10997) · a predicted model of the same protein · chain A against A, TM-score 0.20
  • Q12306 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein SMT3 (Q12306) · a predicted model of the same protein · chain A against A, TM-score 0.19

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