› 4p6e

X-ray diffraction
1.8Å resolution

Crystal Structure of Human Cathepsin S Bound to a Non-covalent Inhibitor

Released:
DOI: 10.2210/pdb4p6e/pdb
PDB entry 4p6e coloured by chain, front view.
PDB entry 4p6e coloured by chain, side view.
PDB entry 4p6e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of Cathepsin S Inhibitor LY3000328 for the Treatment of Abdominal Aortic Aneurysm.
Jadhav PK, Schiffler MA, Gavardinas K, Kim EJ, Matthews DP, Staszak MA, Coffey DS, Shaw BW, Cassidy KC, Brier RA, Zhang Y, Christie RM, Matter WF, Qing K, Durbin JD, Wang Y, Deng GG
ACS Med Chem Lett 5 1138-42 (2014)
PMID: 25313327

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

Assemblies composition:
monomeric (preferred)
homo dimer
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: 230 amino acids
Theoretical weight: 25.65 KDa
Source organism: Homo sapiens
Expression system: Enterobacteria phage L1
UniProt:
  • Canonical: P25774 (Residues: 109-331; Coverage: 71%)
Gene name: CTSS
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand 2FC 2 x 2FC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P4122
Unit cell:
a: 85.692Å b: 85.692Å c: 151.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.199
Expression system: Enterobacteria phage L1

Quick links

Citations

6 review citations

Cysteine Protease Cathepsins in Atherosclerotic Cardiovascular Diseases.
Wu et al. (2018)
5 more

5 mentions without citation

Multiple sites on SARS-CoV-2 spike protein are susceptible to proteolysis by cathepsins B, K, L, S, and V.
Bollavaram et al. (2021)
4 more