› 2bub

X-ray diffraction
2.66Å resolution

Crystal Structure Of Human Dipeptidyl Peptidase IV (CD26) in Complex with a Reversed Amide Inhibitor

Released:
DOI: 10.2210/pdb2bub/pdb
PDB entry 2bub coloured by chain, front view.
PDB entry 2bub coloured by chain, side view.
PDB entry 2bub coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors.
Nordhoff S, Cerezo-Gálvez S, Feurer A, Hill O, Matassa VG, Metz G, Rummey C, Thiemann M, Edwards PJ
Bioorg Med Chem Lett 16 1744-8 (2006)
PMID: 16376544

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151014 (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: Ogataea methanolica
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 FPB 2 x FPB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG
Spacegroup: P212121
Unit cell:
a: 65.486Å b: 66.773Å c: 425.407Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.258 0.329
Expression system: Ogataea methanolica

Quick links

Citations

5 review citations

Fragment-based lead discovery: a chemical update.
Erlanson DA. (2006)
4 more

2 mentions without citation

The good, the bad and the dubious: VHELIBS, a validation helper for ligands and binding sites.
Cereto-Massagué et al. (2013)
1 more