› 1n1m

X-ray diffraction
2.5Å resolution

Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor

Released:
DOI: 10.2210/pdb1n1m/pdb
PDB entry 1n1m coloured by chain, front view.
PDB entry 1n1m coloured by chain, side view.
PDB entry 1n1m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.
Rasmussen HB, Branner S, Wiberg FC, Wagtmann N
Nat Struct Biol 10 19-25 (2003)
PMID: 12483204

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 (8 distinct):
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: 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, NDG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, NDG, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, NDG
Carbohydrate polymer
3 bound ligands:
Ligand NAG 3 x NAG
Ligand HG 4 x HG
Ligand A3M 2 x A3M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711, ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 119.234Å b: 123.448Å c: 131.315Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.263
Expression system: Trichoplusia ni

Quick links

Citations

47 review citations

Molecular physiology and modulation of somatodendritic A-type potassium channels.
Jerng et al. (2004)
46 more

20 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
19 more