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TargetCalcium/calmodulin-dependent protein kinase kinase 2
LigandBDBM50308060
Substrate/Competitorn/a
Meas. Tech.ChEMBL_655710 (CHEMBL1244754)
Kd 15±n/a nM
Citation Zarrinkar, PPGunawardane, RNCramer, MDGardner, MFBrigham, DBelli, BKaraman, MWPratz, KWPallares, GChao, QSprankle, KGPatel, HKLevis, MArmstrong, RCJames, JBhagwat, SS AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML). Blood114:2984-92 (2009) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
Calcium/calmodulin-dependent protein kinase kinase 2
Name:Calcium/calmodulin-dependent protein kinase kinase 2
Synonyms:CAMKK2 | CAMKKB | Calcium/calmodulin-dependent protein kinase kinase 2 (CaMKKB) | Calcium/calmodulin-dependent protein kinase kinase beta | KIAA0787 | KKCC2_HUMAN
Type:Enzyme Catalytic Domain
Mol. Mass.:64746.61
Organism:Homo sapiens (Human)
Description:gi_27437015
Residue:588
Sequence:
MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEP
GCAVDLGLARDRPLEADGQEVPLDTSGSQARPHLSGRKLSLQERSQGGLAAGGSLDMNGR
CICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK
LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAIL
KKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGI
EYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS
ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLK
DLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPS
LATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQP
PGHRPAPRGGGGSALVRGSPCVESCWAPAPGSPARMHPLRPEEAMEPE
Blast this sequence in BindingDB or PDB
  Blast E-value cutoff:
BDBM50308060
n/a
NameBDBM50308060
Synonyms:16-hydroxy-16-(hydroxymethyl)-15-methyl-28-oxa-4,14,19-triazaoctacyclo[12.11.2.1^{15,18}.0^{2,6}.0^{7,27}.0^{8,13}.0^{19,26}.0^{20,25}]octacosa-1(26),2(6),7(27),8(13),9,11,20(25),21,23-nonaen-3-one | CEP-701 | CHEMBL603469 | US11370779, Compound CEP-701
TypeSmall organic molecule
Emp. Form.C26H21N3O4
Mol. Mass.439.4626
SMILESC[C@]12O[C@H](C[C@]1(O)CO)n1c3ccccc3c3c4C(=O)NCc4c4c5ccccc5n2c4c13 |r|
Structure
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