› 3ovz

X-ray diffraction
2.02Å resolution

Cathepsin K in complex with a covalent inhibitor with a ketoamide warhead

Released:
DOI: 10.2210/pdb3ovz/pdb
PDB entry 3ovz coloured by chain, front view.
PDB entry 3ovz coloured by chain, side view.
PDB entry 3ovz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Trifluoromethylphenyl as P2 for ketoamide-based cathepsin S inhibitors.
Cai J, Robinson J, Belshaw S, Everett K, Fradera X, van Zeeland M, van Berkom L, van Rijnsbergen P, Popplestone L, Baugh M, Dempster M, Bruin J, Hamilton W, Kinghorn E, Westwood P, Kerr J, Rankovic Z, Arbuckle W, Bennett DJ, Jones PS, Long C, Martin I, Uitdehaag JC, Meulemans T
Bioorg Med Chem Lett 20 6890-4 (2010)
PMID: 21030256

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 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: 213 amino acids
Theoretical weight: 23.36 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P43235 (Residues: 121-329; Coverage: 67%)
Gene names: CTSK, CTSO, CTSO2
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
Ligand O96 1 x O96
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 55.741Å b: 55.741Å c: 128.916Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.244 0.308
Expression system: Not provided

Quick links

Citations

1 review citation

New drug design with covalent modifiers.
Adeniyi et al. (2016)
5 other articles

5 mentions without citation

Structure Based Docking and Molecular Dynamic Studies of Plasmodial Cysteine Proteases against a South African Natural Compound and its Analogs.
Musyoka et al. (2016)
4 more