X-ray diffraction
2.2Å resolution

Crystal structure of NS-134 in complex with bovine cathepsin B: a two headed epoxysuccinyl inhibitor extends along the whole active site cleft


Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B light chain Chain: A
Molecule details ›
Chain: A
Length: 48 amino acids
Theoretical weight: 5.3 KDa
Source organism: Bos taurus
  • Canonical: P07688 (Residues: 80-127; Coverage: 15%)
Gene name: CTSB
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Cathepsin B heavy chain Chain: B
Molecule details ›
Chain: B
Length: 205 amino acids
Theoretical weight: 22.23 KDa
Source organism: Bos taurus
  • Canonical: P07688 (Residues: 128-332; Coverage: 65%)
Gene name: CTSB
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: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 73.064Å b: 73.064Å c: 141.97Å
α: 90° β: 90° γ: 90°
R R work R free
0.194 0.194 not available