PDBe 1cjl

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF A CYSTEINE PROTEASE PROFORM

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin L1 Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 35.32 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P07711 (Residues: 22-333; Coverage: 99%)
Gene names: CTSL, CTSL1
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 40.08Å b: 88.09Å c: 94.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.241
Expression system: Komagataella pastoris