› 1yk8

X-ray diffraction
2.6Å resolution

Cathepsin K complexed with a cyanamide-based inhibitor

Released:
DOI: 10.2210/pdb1yk8/pdb
PDB entry 1yk8 coloured by chain, front view.
PDB entry 1yk8 coloured by chain, side view.
PDB entry 1yk8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Acyclic cyanamide-based inhibitors of cathepsin K.
Barrett DG, Deaton DN, Hassell AM, McFadyen RB, Miller AB, Miller LR, Payne JA, Shewchuk LM, Willard DH, Wright LL
Bioorg Med Chem Lett 15 3039-43 (2005)
PMID: 15896958

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

1 bound ligand:
Ligand T2M 1 x T2M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P43212
Unit cell:
a: 56.383Å b: 56.383Å c: 128.431Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.277
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

Biochemical properties and regulation of cathepsin K activity.
Lecaille et al. (2008)
1 more