› 3o95

X-ray diffraction
2.85Å 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 tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Dipeptidyl peptidase 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 740 amino acids
Theoretical weight: 85.78 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
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 12 x NAG
Ligand 01T 4 x 01T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P21
Unit cell:
a: 121.718Å b: 123.335Å c: 144.419Å
α: 90° β: 114.78° γ: 90°
R-values:
R R work R free
0.19 0.187 0.248
Expression system: Spodoptera frugiperda

Quick links

Citations

3 review citations

Critical Role of Dipeptidyl Peptidase IV: A Therapeutic Target for Diabetes and Cancer.
De et al. (2019)
2 more

1 mention without citation

Comprehensive analysis of the Co-structures of dipeptidyl peptidase IV and its inhibitor.
Nojima et al. (2016)