› 2rip

X-ray diffraction
2.9Å resolution

Structure of DPPIV in complex with an inhibitor

Released:
DOI: 10.2210/pdb2rip/pdb
PDB entry 2rip coloured by chain, front view.
PDB entry 2rip coloured by chain, side view.
PDB entry 2rip coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and synthesis of potent amido- and benzyl-substituted cis-3-amino-4-(2-cyanopyrrolidide)pyrrolidinyl DPP-IV inhibitors.
Corbett JW, Dirico K, Song W, Boscoe BP, Doran SD, Boyer D, Qiu X, Ammirati M, Vanvolkenburg MA, McPherson RK, Parker JC, Cox ED
Bioorg Med Chem Lett 17 6707-13 (2007)
PMID: 17977724

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 (3 distinct):
Dipeptidyl peptidase 4 Chain: A
Molecule details ›
Chain: A
Length: 729 amino acids
Theoretical weight: 84.58 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P27487 (Residues: 38-766; Coverage: 95%)
Gene names: ADCP2, CD26, DPP4
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 4 x NAG
Ligand 34Q 1 x 34Q
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P43212
Unit cell:
a: 69.22Å b: 69.22Å c: 409.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.293
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes.
Havale et al. (2009)
3 other articles

3 mentions without citation

Identification of novel human dipeptidyl peptidase-IV inhibitors of natural origin (part I): virtual screening and activity assays.
Guasch et al. (2012)
2 more