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Ligands
Code Name Style Show Link
CCZ Phenyl (4-carbamimidoylbenzyl)phosphonate
FMT Formic acid
Non-standard Residues
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Glycosylation
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Code : 3NCL   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor
Release Data : 2011-02-16
Compound :
mol_id molecule chains synonym
1 Suppressor of tumorigenicity 14 protein A Serine protease 14, Matriptase, Membrane-type serine protease 1, MT-SP1, Prostamin, Serine protease TADG-15, Tumor-associated differentially-expressed gene 15 protein
ec: 3.4.21.109
fragment: peptidase S1 domain
mutation: C731S
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: ST14, PRSS14, SNC19, TADG15
Authors : Ray, M., Brown, C., Egea, P.
Keywords : proteinase-inhibitor complex, serine proteinase, benzamidine, phosphonate, serine endopeptidases, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.19 Å )
Citation :

Peptide length and leaving-group sterics influence potency of Peptide phosphonate protease inhibitors.

Brown, C.M.,Ray, M.,Eroy-Reveles, A.A.  et al.
(2011)  Chem.Biol.  18 : 48 - 57

PubMed: 21276938
DOI: 10.1016/j.chembiol.2010.11.007

Chain : A
UniProt : Q9Y5Y6 (ST14_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position. 3.4.21.109 PubMed:16407223
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