X-ray diffraction
2.15Å resolution

Crystal Structure of the tetragonal form of human liver cathepsin B

Source organism: Homo sapiens
Entry authors: Huber CP, Campbell RL, Hasnain S, Hirama T, To R

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)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B light chain Chain: A
Molecule details ›
Chain: A
Length: 47 amino acids
Theoretical weight: 5.21 KDa
Source organism: Homo sapiens
  • Canonical: P07858 (Residues: 80-126; Coverage: 15%)
Gene names: CPSB, CTSB
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Cathepsin B heavy chain Chain: B
Molecule details ›
Chain: B
Length: 205 amino acids
Theoretical weight: 22.44 KDa
Source organism: Homo sapiens
  • Canonical: P07858 (Residues: 129-333; Coverage: 64%)
Gene names: CPSB, CTSB
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43
Unit cell:
a: 85.58Å b: 85.58Å c: 34.39Å
α: 90° β: 90° γ: 90°
R R work R free
0.157 not available not available