› 2ajd

X-ray diffraction
2.56Å resolution

Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)

Released:
DOI: 10.2210/pdb2ajd/pdb
PDB entry 2ajd coloured by chain, front view.
PDB entry 2ajd coloured by chain, side view.
PDB entry 2ajd coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV.
Engel M, Hoffmann T, Manhart S, Heiser U, Chambre S, Huber R, Demuth HU, Bode W
J Mol Biol 355 768-83 (2006)
PMID: 16330047

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 domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-149624 (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: 728 amino acids
Theoretical weight: 84.43 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P22411 (Residues: 39-766; Coverage: 95%)
Gene names: CD26, DPP4
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
3 bound ligands:
Ligand NAG 15 x NAG
Ligand SO4 4 x SO4
Ligand BPR 4 x BPR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P1
Unit cell:
a: 63.4Å b: 122.07Å c: 134.03Å
α: 111.41° β: 95.27° γ: 94.52°
R-values:
R R work R free
0.246 0.246 0.312

Quick links

Citations

7 review citations

DPP4 in Diabetes.
Röhrborn et al. (2015)
6 more