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PDBe Entry: 1mhw 
Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides
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HYDROLASE
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X-RAY DIFFRACTION
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Resolution: 1.9 Å, R-factor: 18.46%, Free R-factor: 22.95%, Spacegroup: P 21 21 21
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11/12/2002, deposition: 21/08/2002, last revision: 24/02/2009
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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.
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Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides
J.MED.CHEM. vol:45, pag:5321-5329 (2002) [PubMed ID 12431059 ]
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Cathepsin L, Cysteine protease, inhibitor complex, x-ray structure, HYDROLASE
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3.4.22.15 ExPASy BRENDA (A C B D)
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Homo sapiens(human) 9606(A B C D)
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Cathepsin L1 precursor (EC 3.4.22.15) (Major excreted protein) (MEP) [Contains: Cathepsin L1 heavy chain; Cathepsin L1 light chain] P07711 (A B C D)
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A, B, C, D, E, F, G, H
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1cjl
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| A, B |
Cathepsin L |
Protein |
P07711 (CATL1_HUMAN)
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175 |
99% |
| C, D |
Cathepsin L |
Protein |
P07711 (CATL1_HUMAN)
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42 |
97% |
| E, F, G, H |
4-biphenylacetyl-Cys-(D)Arg-Tyr-N-(2-phenylethyl) amide |
Mixed |
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5 |
100% |
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