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:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Cathepsin B light chain (preferred)
PDBe Complex ID:
PDB-CPX-139795 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 35.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Cysteine proteinases
Length: 317 amino acids
Theoretical weight: 35.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P07858 (Residues: 18-333; Coverage: 98%)
Sequence domains:
Structure domains: Cysteine proteinases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RUH2R
Spacegroup:
P6522
Expression system: Escherichia coli
