5TDI
Crystal structure of Cathepsin K with a covalently-linked inhibitor at 1.4 Angstrom resolution.
Summary for 5TDI
Entry DOI | 10.2210/pdb5tdi/pdb |
Descriptor | Cathepsin K, 4-fluoro-N-{1-[(Z)-iminomethyl]cyclopropyl}-N~2~-{(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)[1,1'-biphenyl]-4-yl]ethyl }-L-leucinamide (3 entities in total) |
Functional Keywords | cathepsin k, covalent, inhibitor, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 24035.06 |
Authors | Law, S.,Aguda, A.,Nguyen, N.,Brayer, G.,Bromme, D. (deposition date: 2016-09-19, release date: 2017-01-25, Last modification date: 2023-10-04) |
Primary citation | Law, S.,Andrault, P.M.,Aguda, A.H.,Nguyen, N.T.,Kruglyak, N.,Brayer, G.D.,Bromme, D. Identification of mouse cathepsin K structural elements that regulate the potency of odanacatib. Biochem. J., 474:851-864, 2017 Cited by PubMed: 28049758DOI: 10.1042/BCJ20160985 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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