PDBe 1k3b

X-ray diffraction
2.15Å resolution

Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases

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 12-mer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Dipeptidyl peptidase 1 light chain Chain: C
Molecule details ›
Chain: C
Length: 69 amino acids
Theoretical weight: 7.58 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P53634 (Residues: 395-463; Coverage: 16%)
Gene names: CPPI, CTSC
Structure domains: Cysteine proteinases. Chain C
Dipeptidyl peptidase 1 heavy chain Chain: B
Molecule details ›
Chain: B
Length: 164 amino acids
Theoretical weight: 18.49 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P53634 (Residues: 231-394; Coverage: 37%)
Gene names: CPPI, CTSC
Structure domains: Cysteine proteinases
Dipeptidyl peptidase 1 exclusion domain chain Chain: A
Molecule details ›
Chain: A
Length: 119 amino acids
Theoretical weight: 13.5 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P53634 (Residues: 25-143; Coverage: 27%)
Gene names: CPPI, CTSC
Sequence domains: Cathepsin C exclusion domain
Structure domains: Cathepsin C, exclusion domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: I222
Unit cell:
a: 87.154Å b: 88.031Å c: 114.609Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.19 0.231
Expression system: Trichoplusia ni