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TargetProlyl endopeptidase FAP
LigandBDBM50338518
Substrate/Competitorn/a
Meas. Tech.ChEMBL_728477 (CHEMBL1685354)
Ki>30000±n/a nM
Citation Andrews, KMBeebe, DABenbow, JWBoyer, DADoran, SDHui, YLiu, SMcPherson, RKNeagu, CParker, JCPiotrowski, DWSchneider, SRTreadway, JLVanVolkenberg, MAZembrowski, WJ 1-((3S,4S)-4-amino-1-(4-substituted-1,3,5-triazin-2-yl) pyrrolidin-3-yl)-5,5-difluoropiperidin-2-one inhibitors of DPP-4 for the treatment of type 2 diabetes. Bioorg Med Chem Lett21:1810-4 (2011) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
Prolyl endopeptidase FAP
Name:Prolyl endopeptidase FAP
Synonyms:170 kDa melanoma membrane-bound gelatinase | FAP | Fibroblast Activation Protein (FAP) | Fibroblast activation protein alpha | Integral membrane serine protease | SEPR_HUMAN | Seprase
Type:Enzyme
Mol. Mass.:87712.48
Organism:Homo sapiens (Human)
Description:Q12884
Residue:760
Sequence:
MKTWVKIVFGVATSAVLALLVMCIVLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPN
WISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSK
LWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPP
FQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYG
DEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVT
DERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYD
AISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPG
RRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGR
TDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQV
YGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQ
ITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVY
TERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNA
QVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD
Blast this sequence in BindingDB or PDB
  Blast E-value cutoff:
BDBM50338518
n/a
NameBDBM50338518
Synonyms:1-((3S,4S)-4-amino-1-(4-(3,3-difluoropyrrolidin-1-yl)-1,3,5-triazin-2-yl)pyrrolidin-3-yl)-5,5-difluoropiperidin-2-one | CHEMBL1683571
TypeSmall organic molecule
Emp. Form.C16H21F4N7O
Mol. Mass.403.3779
SMILESN[C@H]1CN(C[C@@H]1N1CC(F)(F)CCC1=O)c1ncnc(n1)N1CCC(F)(F)C1 |r|
Structure
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