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5J94

Human cathepsin K mutant C25S in complex with the allosteric effector NSC13345

Replaces:  4LEG
Summary for 5J94
Entry DOI10.2210/pdb5j94/pdb
DescriptorCathepsin K, 2-{[(carbamoylsulfanyl)acetyl]amino}benzoic acid, SULFATE ION, ... (4 entities in total)
Functional Keywordscysteine proteases, allosteric regulation, hydrolase
Biological sourceHomo sapiens (Human)
Cellular locationLysosome: P43235
Total number of polymer chains1
Total formula weight24889.87
Authors
Novinec, M.,Korenc, M.,Lenarcic, B.,Baici, A. (deposition date: 2016-04-08, release date: 2016-04-20, Last modification date: 2024-01-10)
Primary citationNovinec, M.,Korenc, M.,Caflisch, A.,Ranganathan, R.,Lenarcic, B.,Baici, A.
A novel allosteric mechanism in the cysteine peptidase cathepsin K discovered by computational methods.
Nat Commun, 5:3287-, 2014
Cited by
PubMed: 24518821
DOI: 10.1038/ncomms4287
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.22002456664 Å)
Structure validation

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