› 1nu8

X-ray diffraction
2.5Å resolution

Crystal structure of human dipeptidyl peptidase IV (DPP-IV) in complex with Diprotin A (IPI)

Released:
DOI: 10.2210/pdb1nu8/pdb
PDB entry 1nu8 coloured by chain, front view.
PDB entry 1nu8 coloured by chain, side view.
PDB entry 1nu8 coloured by chain, top view.
Source organisms:
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:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151017 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 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: Komagataella pastoris
UniProt:
  • Canonical: P27487 (Residues: 39-766; Coverage: 95%)
Gene names: ADCP2, CD26, DPP4
Sequence domains:
Structure domains:
3-mer peptide Chain: D
Molecule details ›
Chain: D
Length: 3 amino acids
Theoretical weight: 341 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand NAG 8 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 65.136Å b: 67.067Å c: 419.635Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.282
Expression systems:
  • Komagataella pastoris
  • Not provided

Quick links

Citations

22 review citations

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

10 mentions without citation

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
9 more