PDBe 2r6n

X-ray diffraction
1.95Å resolution

Crystal structure of a pyrrolopyrimidine inhibitor in complex with human Cathepsin K

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: 217 amino acids
Theoretical weight: 23.74 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P43235 (Residues: 113-329; 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: ENRAF-NONIUS FR591
Spacegroup: P61
Unit cell:
a: 62.4Å b: 62.4Å c: 121.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.156 0.184
Expression system: Spodoptera frugiperda