› 6b1o

X-ray diffraction
1.91Å 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

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Dipeptidyl peptidase 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 728 amino acids
Theoretical weight: 84.48 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P27487 (Residues: 39-766; Coverage: 95%)
Gene names: ADCP2, CD26, DPP4
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 3 x NAG
Ligand C8S 2 x C8S
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 119.515Å b: 123.342Å c: 130.958Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.202
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

COVID-19 in Elderly Adults: Clinical Features, Molecular Mechanisms, and Proposed Strategies.
Yang et al. (2020)
4 more

2 mentions without citation

A comparative study of the binding properties, dipeptidyl peptidase-4 (DPP-4) inhibitory activity and glucose-lowering efficacy of the DPP-4 inhibitors alogliptin, linagliptin, saxagliptin, sitagliptin and vildagliptin in mice.
Berger et al. (2018)
1 more