› 3g7w

X-ray diffraction
1.75Å resolution

Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein

Released:
DOI: 10.2210/pdb3g7w/pdb
PDB entry 3g7w coloured by chain, front view.
PDB entry 3g7w coloured by chain, side view.
PDB entry 3g7w coloured by chain, top view.
Source organisms:
Primary publication:
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process.
Wiltzius JJ, Sievers SA, Sawaya MR, Eisenberg D
Protein Sci 18 1521-30 (2009)
PMID: 19475663

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-142516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Islet amyloid polypeptide; Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 42.93 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
  • Canonical: P10997 (Residues: 34-55; Coverage: 33%)
Gene names: IAPP, JW3994, b4034, malE
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand SO4 20 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P41212
Unit cell:
a: 84.495Å b: 84.495Å c: 144.292Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.194
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Islet amyloid polypeptide, islet amyloid, and diabetes mellitus.
Westermark et al. (2011)
20 more

3 mentions without citation

Crystal structures of MBP fusion proteins.
Waugh DS. (2016)
2 more