› 2fjp

X-ray diffraction
2.4Å 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 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 6 x NAG
Ligand S14 2 x S14
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P212121
Unit cell:
a: 118.132Å b: 125.577Å c: 137.068Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.194 0.24
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

Plasma protein binding: from discovery to development.
Bohnert et al. (2013)
4 more

7 mentions without citation

Ligand deconstruction: Why some fragment binding positions are conserved and others are not.
Kozakov et al. (2015)
6 more