PDBe 3k9m

X-ray diffraction
2.61Å resolution

Cathepsin B in complex with stefin A

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa 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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cystatin-A Chains: C, D
Molecule details ›
Chains: C, D
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%)
Gene names: CSTA, STF1, STFA
Sequence domains: Cystatin domain
Structure domains: Nuclear Transport Factor 2; Chain: A,
Cathepsin B Chains: A, B
Molecule details ›
Chains: A, B
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%)
Gene names: CPSB, CTSB
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P1
Unit cell:
a: 62.122Å b: 31.078Å c: 70.937Å
α: 89.95° β: 104.45° γ: 89.9°
R-values:
R R work R free
0.201 0.198 0.25
Expression system: Escherichia coli