Brand  (β version)

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain:

Ligands
Code Name Link
C4P N-[(1r)-2-(benzylsulfanyl)-1-formylethyl]-N-(morpholin-4-ylcarbonyl)-L-phenylalaninamide
Code : 1NQC
Header : HYDROLASE
Title : Crystal structures of Cathepsin S inhibitor complexes
Release Data : 2003-04-15
Compound :
mol_id molecule chains
1 Cathepsin S A
ec: 3.4.22.27
Source :
mol_id organism_scientific organism_common
1 Homo sapiens  (taxid:9606) Human
Authors : Pauly, T.A., Sulea, T., Ammirati, M., Sivaraman, J., Danley, D.E., Griffor, M.C., Kamath, A.V., Wang, I.K., Laird, E.R., Menard, R., Cygler, M., Rath, V.L.
Keywords : Antigen presentation, binding specificity, cysteine proteases, inhibitor complexes, structure-based design, structural plasticity, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.8 Å )
Citation :

Specificity determinants of human cathepsin s revealed by crystal structures of complexes.

Pauly, T.A.,Sulea, T.,Ammirati, M.  et al.
(2003)  Biochemistry  42 : 3203 - 3213

PubMed: 12641451
DOI: 10.1021/bi027308i

Chain : A
UniProt : P25774 (CATS_HUMAN)
Reaction : Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val- Arg-|-Xaa compound.