Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
C4P N-[(1r)-2-(benzylsulfanyl)-1-formylethyl]-N-(morpholin-4-ylcarbonyl)-L-phenylalaninamide
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1NQC   PDBj   RCSB PDB   PDBe
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: EC: Evidence:
Physiological Direction:
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. 3.4.22.27 -
-