› 4ebb

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-193753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dipeptidyl peptidase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 472 amino acids
Theoretical weight: 52.84 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: Q9UHL4 (Residues: 27-492; Coverage: 99%)
Gene names: DPP2, DPP7, QPP
Sequence domains: Serine carboxypeptidase S28
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAG 3 x NAG
Ligand ZN 3 x ZN
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 61.089Å b: 96.447Å c: 192.137Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.23
Expression system: Cricetulus griseus

Quick links

Citations

6 review citations

The Dipeptidyl Peptidase Family, Prolyl Oligopeptidase, and Prolyl Carboxypeptidase in the Immune System and Inflammatory Disease, Including Atherosclerosis.
Waumans et al. (2015)
5 more

3 mentions without citation

Structures of human DPP7 reveal the molecular basis of specific inhibition and the architectural diversity of proline-specific peptidases.
Bezerra et al. (2012)
2 more