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Ligands
Code Name Style Show Link
0IW Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-[(3s)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-phenylalaninamide
SO4 Sulfate ion
Non-standard Residues
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Code : 1FH0   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE inhibitor
Title : CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR
Release Data : 2001-07-30
Compound :
mol_id molecule chains synonym
1 CATHEPSIN V A,B CATHEPSIN L2
ec: 3.4.22.-
mutation: N108Q, N178D
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Saccharomyces cerevisiae  (taxid:4932)
expression_system_common: Baker's yeast
Authors : Somoza, J.R.
Keywords : cathepsin, papain, protease, cancer, HYDROLASE-HYDROLASE inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 1.6 Å )
Citation :

Crystal structure of human cathepsin V.

Somoza, J.R.,Zhan, H.,Bowman, K.K.  et al.
(2000)  Biochemistry  39 : 12543 - 12551

PubMed: 11027133
DOI: 10.1021/bi000951p

Chain : A, B
UniProt : O60911 (CATL2_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec). 3.4.22.43 PubMed:10029531
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