› 2o6x

X-ray diffraction
1.4Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173201 (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

Quick links

Citations

7 review citations

Cysteine Proteases: Modes of Activation and Future Prospects as Pharmacological Targets.
Verma et al. (2016)
6 more

23 mentions without citation

Structural and functional relationships in the virulence-associated cathepsin L proteases of the parasitic liver fluke, Fasciola hepatica.
Stack et al. (2008)
22 more