1MHW
Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides
Summary for 1MHW
Entry DOI | 10.2210/pdb1mhw/pdb |
Related | 1CJL |
Related PRD ID | PRD_000270 |
Descriptor | Cathepsin L, 4-biphenylacetyl-Cys-(D)Arg-Tyr-N-(2-phenylethyl) amide, ... (4 entities in total) |
Functional Keywords | cathepsin l, cysteine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Homo sapiens (human) More |
Cellular location | Lysosome: P07711 P07711 |
Total number of polymer chains | 8 |
Total formula weight | 50780.57 |
Authors | Chowdhury, S.,Sivaraman, J.,Wang, J.,Devanathan, G.,Lachance, P.,Qi, H.,Menard, R.,Lefebvre, J.,Konishi, Y.,Cygler, M.,Sulea, T.,Purisima, E.O. (deposition date: 2002-08-21, release date: 2002-12-11, Last modification date: 2017-10-11) |
Primary citation | Chowdhury, S.,Sivaraman, J.,Wang, J.,Devanathan, G.,Lachance, P.,Qi, H.,Menard, R.,Lefebvre, J.,Konishi, Y.,Cygler, M.,Sulea, T.,Purisima, E.O. Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides J.Med.Chem., 45:5321-5329, 2002 Cited by PubMed: 12431059DOI: 10.1021/jm020238t PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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