PDBe 3h89

X-ray diffraction
2.5Å resolution

A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 4)


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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Cathepsin L1 heavy chain Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 220 amino acids
Theoretical weight: 24.19 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
  • Canonical: P07711 (Residues: 114-333; Coverage: 70%)
Gene names: CTSL, CTSL1
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 99.404Å b: 61.075Å c: 205.184Å
α: 90° β: 89.91° γ: 90°
R R work R free
0.22 0.22 0.28
Expression system: Saccharomyces cerevisiae