PDBe 3h8b

X-ray diffraction
1.8Å resolution

A combined crystallographic and molecular dynamics study of cathepsin-L retro-binding inhibitors(compound 9)

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 61.99Å b: 99.234Å c: 206.462Å
α: 90° β: 90.05° γ: 90°
R-values:
R R work R free
0.216 0.216 0.25
Expression system: Saccharomyces cerevisiae