2dc9

X-ray diffraction
1.94Å resolution

X-ray crystal structure analysis of bovine spleen cathepsin B-CA074Me complex

Released:
Source organism: Bos taurus
Entry author: Watanabe D

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B Chain: A
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 27.92 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P07688 (Residues: 80-335; Coverage: 81%)
Gene name: CTSB
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 72.32Å b: 72.32Å c: 139.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.221