PDBe 1au3

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF THE CYSTEINE PROTEASE HUMAN CATHEPSIN K IN COMPLEX WITH A COVALENT PYRROLIDINONE INHIBITOR

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin K Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 23.52 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P43235 (Residues: 115-329; Coverage: 69%)
Gene names: CTSK, CTSO, CTSO2
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P212121
Unit cell:
a: 38.84Å b: 50.99Å c: 103.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.353
Expression system: Spodoptera frugiperda