› 1cte

X-ray diffraction
2.1Å resolution

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

Released:
DOI: 10.2210/pdb1cte/pdb
PDB entry 1cte coloured by chain, front view.
PDB entry 1cte coloured by chain, side view.
PDB entry 1cte 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: 254 amino acids
Theoretical weight: 27.74 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00787 (Residues: 80-333; Coverage: 79%)
Gene name: Ctsb
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
Ligand PYS 2 x PYS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 47.07Å b: 90.19Å c: 62.21Å
α: 90° β: 97.43° γ: 90°
R-values:
R R work R free
0.166 0.166 not available
Expression system: Saccharomyces cerevisiae

Quick links

Citations

1 review citation

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

3 mentions without citation

Crystal Structures of TbCatB and rhodesain, potential chemotherapeutic targets and major cysteine proteases of Trypanosoma brucei.
Kerr et al. (2010)
2 more