› 1q6k

X-ray diffraction
2.1Å resolution

Cathepsin K complexed with t-butyl(1S)-1-cyclohexyl-2-oxoethylcarbamate

Released:
DOI: 10.2210/pdb1q6k/pdb
PDB entry 1q6k coloured by chain, front view.
PDB entry 1q6k coloured by chain, side view.
PDB entry 1q6k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Exploration of the P1 SAR of aldehyde cathepsin K inhibitors.
Catalano JG, Deaton DN, Furfine ES, Hassell AM, McFadyen RB, Miller AB, Miller LR, Shewchuk LM, Willard DH, Wright LL
Bioorg Med Chem Lett 14 275-8 (2004)
PMID: 14684342

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154996 (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

2 bound ligands:
Ligand SO4 1 x SO4
Ligand TCO 1 x TCO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 56.443Å b: 56.443Å c: 130.212Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 not available not available
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

Cathepsin K inhibitors for osteoporosis and potential off-target effects.
Brömme et al. (2009)
1 more

2 mentions without citation

Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding.
Chruszcz et al. (2009)
1 more