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TitleAn allosteric site enables fine-tuning of cathepsin K by diverse effectors.
Journal, issue, pagesFEBS Lett., Vol. 590, Page 4507-4518, Year 2016
Publish dateApr 12, 2016 (structure data deposition date)
AuthorsNovinec, M. / Rebernik, M. / Lenarcic, B.
External linksFEBS Lett. / PubMed:27859061
MethodsX-ray diffraction
Resolution1.61 - 1.75 Å
Structure data

PDB-5ja7:
Human cathepsin K mutant C25S in complex with the allosteric effector NSC94914
Method: X-RAY DIFFRACTION / Resolution: 1.61 Å

PDB-5jh3:
Human cathepsin K mutant C25S
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-6HM:
[([1,1'-biphenyl]-2-yl)methyl]propanedioic acid

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / allostery cysteine peptidase proteolysis enzyme regulation collagenase / allostery cysteine / peptidase proteolysis / enzyme regulation / collagenase

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