› 1the

X-ray diffraction
1.9Å resolution

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

Released:
DOI: 10.2210/pdb1the/pdb
PDB entry 1the coloured by chain, front view.
PDB entry 1the coloured by chain, side view.
PDB entry 1the coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
Jia Z, Hasnain S, Hirama T, Lee X, Mort JS, To R, Huber CP
J Biol Chem 270 5527-33 (1995)
PMID: 7890671

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133552 (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

1 bound ligand:
Ligand 0E6 2 x 0E6
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 47.11Å b: 90.15Å c: 62.31Å
α: 90° β: 97.24° γ: 90°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Saccharomyces cerevisiae

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Citations

1 review citation

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
Khan et al. (1998)
53 other articles

7 mentions without citation

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O'Toole et al. (2012)
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