› 3n4c

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|- compound.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin S Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 24.01 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P25774 (Residues: 115-331; Coverage: 69%)
Gene name: CTSS
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

3 bound ligands:
Ligand EF3 2 x EF3
Ligand DMS 2 x DMS
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P4122
Unit cell:
a: 85.629Å b: 85.629Å c: 150.573Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.249 0.286
Expression system: Trichoplusia ni

Quick links

Citations

5 review citations

Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors.
Siklos et al. (2015)
4 more

1 mention without citation

Calculate protein-ligand binding affinities with the extended linear interaction energy method: application on the Cathepsin S set in the D3R Grand Challenge 3.
He et al. (2019)