8b5f

X-ray diffraction
1.7Å resolution

Human cathepsin B in complex with the carbamate inhibitor 31

Released:
Source organism: Homo sapiens
Entry authors: Rubesova P, Guetschow M, Mares M

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-139795 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B Chain: A
Molecule details ›
Chain: A
Length: 255 amino acids
Theoretical weight: 27.96 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P07858 (Residues: 79-333; Coverage: 79%)
Gene names: CPSB, CTSB
Sequence domains: Papain family cysteine protease

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 30.573Å b: 81.565Å c: 93.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.205
Expression system: Komagataella pastoris