› 3fr1

X-ray diffraction
1.85Å resolution

NFLVHS segment from Islet Amyloid Polypeptide (IAPP or Amylin)

Released:
DOI: 10.2210/pdb3fr1/pdb
PDB entry 3fr1 coloured by chain, front view.
PDB entry 3fr1 coloured by chain, side view.
PDB entry 3fr1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular mechanisms for protein-encoded inheritance.
Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D
Nat Struct Mol Biol 16 973-8 (2009)
PMID: 19684598

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Islet amyloid polypeptide Chain: A
Molecule details ›
Chain: A
Length: 6 amino acids
Theoretical weight: 717 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P10997 (Residues: 47-52; Coverage: 9%)
Gene name: IAPP

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 11.48Å b: 9.552Å c: 38.582Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.192 0.232
Expression system: Not provided

Quick links

Citations

40 review citations

The amyloid state of proteins in human diseases.
Eisenberg et al. (2012)
39 more

5 mentions without citation

Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective.
Hassan et al. (2022)
4 more