› 5mbm

X-ray diffraction
2.76Å resolution

Cathepsin B in complex with DARPin 8h6

Released:
DOI: 10.2210/pdb5mbm/pdb
PDB entry 5mbm coloured by chain, front view.
PDB entry 5mbm coloured by chain, side view.
PDB entry 5mbm coloured by chain, top view.
Source organisms:
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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139798 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B Chains: A, B
Molecule details ›
Chains: A, B
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 8h6 Chains: C, D
Molecule details ›
Chains: C, D
Length: 171 amino acids
Theoretical weight: 18.16 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand SCH 2 x SCH

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21212
Unit cell:
a: 101.45Å b: 201.52Å c: 46.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.281 0.256 0.281
Expression system: Escherichia coli

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