PDBe 3of9

X-ray diffraction
1.76Å resolution

Structural Basis for Irreversible Inhibition of Human Cathepsin L by a Diazomethylketone 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: 221 amino acids
Theoretical weight: 24.32 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P07711 (Residues: 113-333; 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 X29A
Spacegroup: P65
Unit cell:
a: 85.557Å b: 85.557Å c: 50.201Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.224 0.249
Expression system: Komagataella pastoris