3bc3

X-ray diffraction
2.2Å resolution

Exploring inhibitor binding at the S subsites of cathepsin L

Released:

Function and Biology Details

Reaction catalysed:
Similar 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)
Assembly name:
PDBe Complex ID:
PDB-CPX-139718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin L Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 24.22 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
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

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2221
Unit cell:
a: 74.765Å b: 90.929Å c: 126.026Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.234
Expression system: Komagataella pastoris