› 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

49 review citations

Structure, Function, and Evolution of Coronavirus Spike Proteins.
Li F. (2016)
48 more

20 mentions without citation

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