PDBe 1cpj

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa 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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 28.44 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00787 (Residues: 74-333; Coverage: 81%)
Gene name: Ctsb
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 47.09Å b: 90.25Å c: 62.1Å
α: 90° β: 97.29° γ: 90°
R-values:
R R work R free
0.175 0.175 not available
Expression system: Saccharomyces cerevisiae