PDBe 2o6x

X-ray diffraction
1.4Å resolution

Crystal Structure of ProCathepsin L1 from Fasciola hepatica

Released:

Function and Biology Details

Reaction catalysed:
Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin L-like proteinase Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 35.11 KDa
Source organism: Fasciola hepatica
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q24940 (Residues: 17-326; Coverage: 100%)
Gene name: Cat-1
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21212
Unit cell:
a: 57.271Å b: 105.961Å c: 49.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.128 0.165
Expression system: Komagataella pastoris