› 2oae

X-ray diffraction
3Å resolution

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-147060 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dipeptidyl peptidase 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 730 amino acids
Theoretical weight: 84.34 KDa
Source organism: Rattus norvegicus
UniProt:
  • Canonical: P14740 (Residues: 38-767; Coverage: 95%)
Gene names: Cd26, Dpp4
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand AIL 1 x AIL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P213
Unit cell:
a: 208.349Å b: 208.349Å c: 208.349Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.249 0.28

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Citations

4 review citations

Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes.
Havale et al. (2009)
3 more