PDBe 1huc

X-ray diffraction
2.1Å resolution

THE REFINED 2.15 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF HUMAN LIVER CATHEPSIN B: THE STRUCTURAL BASIS FOR ITS SPECIFICITY

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:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin B light chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 47 amino acids
Theoretical weight: 5.21 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • 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 Chains: B, D
Molecule details ›
Chains: B, D
Length: 205 amino acids
Theoretical weight: 22.44 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P07858 (Residues: 129-333; Coverage: 64%)
Gene names: CPSB, CTSB
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 86.23Å b: 34.16Å c: 85.56Å
α: 90° β: 102.9° γ: 90°
R-values:
R R work R free
0.164 not available not available
Expression system: Not provided