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TargetDipeptidyl peptidase 9
LigandBDBM50328796
Substrate/Competitorn/a
Meas. Tech.ChEMBL_673773 (CHEMBL1274950)
Ki>30000±n/a nM
Citation O'Connor, SPWang, YSimpkins, LMBrigance, RPMeng, WWang, AKirby, MSWeigelt, CAHamann, LG Synthesis, SAR, and atropisomerism of imidazolopyrimidine DPP4 inhibitors. Bioorg Med Chem Lett20:6273-6 (2010) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
Dipeptidyl peptidase 9
Name:Dipeptidyl peptidase 9
Synonyms:DPP9 | DPP9_HUMAN | DPRP-2 | DPRP2 | Dipeptidyl peptidase 9 (DDP9) | Dipeptidyl peptidase 9 (DPP-9) | Dipeptidyl peptidase 9 (DPP9) | Dipeptidyl peptidase IV-related protein 2 | Dipeptidyl peptidase IX | Dipeptidyl peptidase IX (DDP-IX) | Dipeptidyl peptidase-like protein 9
Type:Enzyme
Mol. Mass.:98260.70
Organism:Homo sapiens (Human)
Description:Q86TI2
Residue:863
Sequence:
MATTGTPTADRGDAAATDDPAARFQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQ
KTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGV
YSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEI
KTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGLSNVLDDPKSAG
VATFVIQEEFDRFTGYWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKT
DSYRYPRTGSKNPKIALKLAEFQTDSQGKIVSTQEKELVQPFSSLFPKVEYIARAGWTRD
GKYAWAMFLDRPQQWLQLVLLPPALFIPSTENEEQRLASARAVPRNVQPYVVYEEVTNVW
INVHDIFYPFPQSEGEDELCFLRANECKTGFCHLYKVTAVLKSQGYDWSEPFSPGEDEFK
CPIKEEIALTSGEWEVLARHGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR
LTTPGFSHSCSMSQNFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAAS
CPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIK
YLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFID
LSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHG
YEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERH
SIRCPESGEHYEVTLLHFLQEYL
Blast this sequence in BindingDB or PDB
  Blast E-value cutoff:
BDBM50328796
n/a
NameBDBM50328796
Synonyms:(5-(3-fluoro-4-(trifluoromethyl)phenyl)-2-(2-methoxyphenyl)-7-methylimidazo[1,2-a]pyrimidin-6-yl)methanamine | CHEMBL1271065
TypeSmall organic molecule
Emp. Form.C22H18F4N4O
Mol. Mass.430.3981
SMILESCOc1ccccc1-c1cn2c(-c3ccc(c(F)c3)C(F)(F)F)c(CN)c(C)nc2n1
Structure
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