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 heavy chain (preferred)
PDBe Complex ID:
PDB-CPX-139796 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B light chain
Molecule details ›
Chains: A, D
Length: 47 amino acids
Theoretical weight: 5.21 KDa
Source organism: Homo sapiens
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 47 amino acids
Theoretical weight: 5.21 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P07858 (Residues: 80-126; Coverage: 15%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Cathepsin B heavy chain
Molecule details ›
Chains: B, E
Length: 205 amino acids
Theoretical weight: 22.44 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Length: 205 amino acids
Theoretical weight: 22.44 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P07858 (Residues: 129-333; Coverage: 64%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
