4yv8

X-ray diffraction
2Å resolution

Crystal structure of cathepsin K bound to the covalent inhibitor lichostatinal

Released:

Function and Biology Details

Reaction catalysed:
Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-154998 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin K Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 23.52 KDa
Source organism: Homo sapiens
Expression system: Pichia
UniProt:
  • Canonical: P43235 (Residues: 115-329; Coverage: 69%)
Gene names: CTSK, CTSO, CTSO2
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Lichostatinal Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 500 Da
Source organism: actinomycete 095-35

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P43212
Unit cell:
a: 56.717Å b: 56.717Å c: 130.365Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.205
Expression system: Pichia