› 2hh5

X-ray diffraction
1.8Å resolution

Crystal Structure of Cathepsin S in complex with a Zinc mediated non-covalent arylaminoethyl amide

Released:
DOI: 10.2210/pdb2hh5/pdb
PDB entry 2hh5 coloured by chain, front view.
PDB entry 2hh5 coloured by chain, side view.
PDB entry 2hh5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis and SAR of arylaminoethyl amides as noncovalent inhibitors of cathepsin S: P3 cyclic ethers.
Tully DC, Liu H, Chatterjee AK, Alper PB, Epple R, Williams JA, Roberts MJ, Woodmansee DH, Masick BT, Tumanut C, Li J, Spraggon G, Hornsby M, Chang J, Tuntland T, Hollenbeck T, Gordon P, Harris JL, Karanewsky DS
Bioorg Med Chem Lett 16 5112-7 (2006)
PMID: 16876402

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 domain:

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: 220 amino acids
Theoretical weight: 24.39 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P25774 (Residues: 112-331; Coverage: 70%)
Gene name: CTSS
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

3 bound ligands:
Ligand ZN 6 x ZN
Ligand CL 2 x CL
Ligand GNQ 2 x GNQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: R3
Unit cell:
a: 109.542Å b: 109.542Å c: 98.529Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.173 0.22
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Cathepsin S inhibitors: 2004-2010.
Lee-Dutra et al. (2011)
9 other articles

3 mentions without citation

Zinc-binding cysteines: diverse functions and structural motifs.
Pace et al. (2014)
2 more