PDBe 1by8

X-ray diffraction
2.6Å resolution

THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K

Released:
Source organism: Homo sapiens

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin K Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 35.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43235 (Residues: 16-329; Coverage: 100%)
Gene names: CTSK, CTSO, CTSO2
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: C2221
Unit cell:
a: 56.78Å b: 156.55Å c: 96.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.344
Expression system: Escherichia coli