› 1nu6

X-ray diffraction
2.1Å resolution

Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)

Released:
DOI: 10.2210/pdb1nu6/pdb
PDB entry 1nu6 coloured by chain, front view.
PDB entry 1nu6 coloured by chain, side view.
PDB entry 1nu6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV.
Thoma R, Löffler B, Stihle M, Huber W, Ruf A, Hennig M
Structure 11 947-59 (2003)
PMID: 12906826

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
Macromolecule:
Dipeptidyl peptidase 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 728 amino acids
Theoretical weight: 84.46 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P27487 (Residues: 39-766; Coverage: 95%)
Gene names: ADCP2, CD26, DPP4
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAG 8 x NAG
Ligand HG 6 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 65.496Å b: 68.24Å c: 419.289Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.215 0.266
Expression system: Komagataella pastoris

Quick links

Citations

26 review citations

The metabolic serine hydrolases and their functions in mammalian physiology and disease.
Long et al. (2011)
25 more

7 mentions without citation

Protein subunit interfaces: heterodimers versus homodimers.
Zhanhua et al. (2005)
6 more