PDBe 4cdd

X-ray diffraction
2.35Å resolution

Human DPP1 in complex with (2S)-N-((1S)-1-cyano-2-(4-(4-cyanophenyl) phenyl)ethyl)piperidine-2-carboxamide

Released:

Function and Biology Details

Reaction catalysed:
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Dipeptidyl peptidase 1 heavy chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 165 amino acids
Theoretical weight: 18.63 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P53634 (Residues: 230-394; Coverage: 38%)
Gene names: CPPI, CTSC
Structure domains: Cysteine proteinases
Dipeptidyl peptidase 1 light chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 69 amino acids
Theoretical weight: 7.58 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P53634 (Residues: 395-463; Coverage: 16%)
Gene names: CPPI, CTSC
Structure domains: Cysteine proteinases. Chain C
Dipeptidyl peptidase 1 exclusion domain chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 120 amino acids
Theoretical weight: 13.6 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P53634 (Residues: 25-144; Coverage: 27%)
Gene names: CPPI, CTSC
Sequence domains: Cathepsin C exclusion domain
Structure domains: Dipeptidyl peptidase I (cathepsin C), exclusion domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P3121
Unit cell:
a: 84.291Å b: 84.291Å c: 221.114Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.223
Expression system: Spodoptera frugiperda