| Reaction Details |
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 | Report a problem with these data |
| Target | Leucine-rich repeat serine/threonine-protein kinase 2 [970-2527] |
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| Ligand | BDBM13530 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | LRRK2 Kinase Assay |
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| pH | 7.4±n/a |
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| Temperature | 298.15±n/a K |
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| IC50 | 8.3e+3± 1.2e+3 nM |
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| Comments | extracted |
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| Citation |  Ray, S; Bender, S; Kang, S; Lin, R; Glicksman, MA; Liu, M The Parkinson disease-linked LRRK2 protein mutation I2020T stabilizes an active state conformation leading to increased kinase activity. J Biol Chem289:13042-53 (2014) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Leucine-rich repeat serine/threonine-protein kinase 2 [970-2527] |
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| Name: | Leucine-rich repeat serine/threonine-protein kinase 2 [970-2527] |
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| Synonyms: | LRRK2 | LRRK2_HUMAN | Leucine-rich repeat kinase 2 (LRRK2 t-WT) | Leucine-rich repeat serine/threonine-protein kinase 2 (LRRK2) | PARK8 |
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| Type: | Protein |
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| Mol. Mass.: | 177317.56 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Human LRRK2 variant (970-2527aa) |
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| Residue: | 1558 |
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| Sequence: | HSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQ
LCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFN
LSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFL
EACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQ
YLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLEN
LTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKA
VPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLV
LNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVIL
VGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESL
NFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENEL
PHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRR
DVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSE
IIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCL
VGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLK
KWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIM
LNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHH
PSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAM
IIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVI
YNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEK
LIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWL
GCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINT
EDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLK
ILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAF
SDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMS
YSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNV
MLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE
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| BDBM13530 |
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| n/a |
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| Name | BDBM13530 |
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| Synonyms: | 4-[(4-methylpiperazin-1-yl)methyl]-N-[4-methyl-3-[(4-pyridin-3-ylpyrimidin-2-yl)amino]phenyl]benzamide | CHEMBL941 | Gleevec | Imatinib | Imatinib, 21 | N-(4-methyl-3-{[4-(pyridin-3-yl)pyrimidin-2-yl]amino}phenyl)-4-[(4-methylpiperazin-1-yl)methyl]benzamide | STI-571 | STI571 | US10906896, Cpd imatinib | US11649218, Example Imatinib | US11725005, Compound imatinib | US9255107, Imatinib | cid_5291 | imatinib-CD3 | med.21724, Compound 6 |
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| Type | Small organic molecule |
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| Emp. Form. | C29H31N7O |
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| Mol. Mass. | 493.6027 |
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| SMILES | CN1CCN(Cc2ccc(cc2)C(=O)Nc2ccc(C)c(Nc3nccc(n3)-c3cccnc3)c2)CC1 |
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| Structure | 
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