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:
hetero dimer (preferred)
Assembly name:
Cathepsin B (preferred)
PDBe Complex ID:
PDB-CPX-139699 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B light chain
Molecule details ›
Chain: A
Length: 48 amino acids
Theoretical weight: 5.3 KDa
Source organism: Bos taurus
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 48 amino acids
Theoretical weight: 5.3 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P07688 (Residues: 80-127; Coverage: 15%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Cathepsin B heavy chain
Molecule details ›
Chain: B
Length: 205 amino acids
Theoretical weight: 22.23 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Length: 205 amino acids
Theoretical weight: 22.23 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P07688 (Residues: 128-332; Coverage: 65%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
