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:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Cathepsin-B - cystatin-A complex (preferred)
PDBe Complex ID:
PDB-CPX-133896 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 27.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Length: 254 amino acids
Theoretical weight: 27.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P07858 (Residues: 80-333; Coverage: 79%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Cystatin-A
Molecule details ›
Chains: C, D
Length: 98 amino acids
Theoretical weight: 11.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Cystatin domain
Structure domains: Nuclear Transport Factor 2; Chain: A,
Length: 98 amino acids
Theoretical weight: 11.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P01040 (Residues: 1-98; Coverage: 100%)
Sequence domains: Cystatin domain
Structure domains: Nuclear Transport Factor 2; Chain: A,
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ELETTRA BEAMLINE 5.2R
Spacegroup:
P1
Expression system: Escherichia coli
