1r9m

X-ray diffraction
2.1Å resolution

Crystal Structure of Human Dipeptidyl Peptidase IV at 2.1 Ang. Resolution.

Released:

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:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Dipeptidyl peptidase 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 733 amino acids
Theoretical weight: 85.15 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
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 : NEW Components: NAG, MAN
Carbohydrate polymer : NEW Components: NAG, MAN
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P21
Unit cell:
a: 121.823Å b: 124.056Å c: 144.491Å
α: 90° β: 114.71° γ: 90°
R-values:
R R work R free
0.219 0.218 0.249
Expression system: Trichoplusia ni