PDBe 2xu5

X-ray diffraction
1.6Å resolution

CATHEPSIN L WITH A NITRILE INHIBITOR

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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin L1 heavy chain Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 24.19 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

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 36.943Å b: 59.107Å c: 89.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.276
Expression system: Escherichia coli