› 1jqp

X-ray diffraction
2.4Å resolution

dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family

Released:
DOI: 10.2210/pdb1jqp/pdb
PDB entry 1jqp coloured by chain, front view.
PDB entry 1jqp coloured by chain, side view.
PDB entry 1jqp coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain.
Olsen JG, Kadziola A, Lauritzen C, Pedersen J, Larsen S, Dahl SW
FEBS Lett 506 201-6 (2001)
PMID: 11602245

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-550832 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dipeptidyl peptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 438 amino acids
Theoretical weight: 49.87 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P80067 (Residues: 25-462; Coverage: 100%)
Gene name: Ctsc
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NAG 2 x NAG
Ligand CL 1 x CL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P6422
Unit cell:
a: 166.24Å b: 166.24Å c: 80.48Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.245 0.245 0.274
Expression system: Spodoptera frugiperda

Quick links

Citations

3 review citations

Cysteine cathepsins: from structure, function and regulation to new frontiers.
Turk et al. (2012)
2 more

1 mention without citation

Characterization of P. falciparum dipeptidyl aminopeptidase 3 specificity identifies differences in amino acid preferences between peptide-based substrates and covalent inhibitors.
de Vries et al. (2019)