PDBe 1pbh

X-ray diffraction
3.2Å resolution

CRYSTAL STRUCTURE OF HUMAN RECOMBINANT PROCATHEPSIN B AT 3.2 ANGSTROM RESOLUTION

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B Chain: A
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 35.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07858 (Residues: 18-333; Coverage: 98%)
Gene names: CPSB, CTSB
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 44.95Å b: 77.1Å c: 97.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.252
Expression system: Escherichia coli