5mbl

X-ray diffraction
1.81Å resolution

Cathepsin B in complex with DARPin 81

Released:
Entry authors: Turk D, Kramer L, Renko M, Turk B

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B Chain: A
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 28.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07858 (Residues: 78-333; Coverage: 80%)
Gene names: CPSB, CTSB
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
DARPin 81 Chain: B
Molecule details ›
Chain: B
Length: 171 amino acids
Theoretical weight: 17.87 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P42212
Unit cell:
a: 105.79Å b: 105.79Å c: 92.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 0.193
Expression system: Escherichia coli