PDBe 3hha

X-ray diffraction
1.27Å resolution

Crystal structure of cathepsin L in complex with AZ12878478

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:
  • not assigned

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin L1 heavy chain Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 220 amino acids
Theoretical weight: 24.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07711 (Residues: 114-333; Coverage: 70%)
Gene names: CTSL, CTSL1
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 57.26Å b: 62.69Å c: 68.24Å
α: 105.6° β: 93.22° γ: 115.55°
R-values:
R R work R free
0.117 0.116 0.152
Expression system: Escherichia coli