5ja7

X-ray diffraction
1.61Å resolution

Human cathepsin K mutant C25S in complex with the allosteric effector NSC94914

Released:
Source organism: Homo sapiens
Primary publication:
An allosteric site enables fine-tuning of cathepsin K by diverse effectors.
FEBS Lett 590 4507-4518 (2016)
PMID: 27859061

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-154996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin K Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 24.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43235 (Residues: 107-329; Coverage: 71%)
Gene names: CTSK, CTSO, CTSO2
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21
Unit cell:
a: 31.62Å b: 74.07Å c: 90.04Å
α: 90° β: 99.29° γ: 90°
R-values:
R R work R free
0.183 0.181 0.22
Expression system: Escherichia coli