Reaction Details |
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Target | DNA ligase 1 |
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Ligand | BDBM23099 |
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Substrate/Competitor | BDBM23028 |
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Meas. Tech. | FAAH Inhibition Assay |
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Temperature | 298.15±n/a K |
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Ki | 7±n/a nM |
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Comments | extracted |
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Citation | Hardouin, C; Kelso, MJ; Romero, FA; Rayl, TJ; Leung, D; Hwang, I; Cravatt, BF; Boger, DL Structure-activity relationships of alpha-ketooxazole inhibitors of fatty acid amide hydrolase. J Med Chem50:3359-68 (2007) [PubMed] Article |
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More Info.: | Get all data from this article, Solution Info, Assay Method |
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DNA ligase 1 |
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Name: | DNA ligase 1 |
Synonyms: | ATP-dependent DNA ligase | DNA Ligase I | DNLI1_HUMAN | Fatty Acid Amide Hydrolase | LIG1 | Polydeoxyribonucleotide synthase [ATP] |
Type: | Enzyme |
Mol. Mass.: | 101721.76 |
Organism: | Homo sapiens (Human) |
Description: | n/a |
Residue: | 919 |
Sequence: | MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKA
ARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPK
RRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQ
PTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVK
KEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIE
EVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQ
ATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSAST
AKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAM
VDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPL
KPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPD
IISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAF
DLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCE
GLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLL
ASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSA
VWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQ
SQIQNQQGEDSGSDPEDTY
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BDBM23099 |
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BDBM23028 |
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Name | BDBM23099 |
Synonyms: | 7-(3-chlorophenyl)-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]hept-6-yn-1-one | alpha-ketooxazole, 4hh |
Type | Small organic molecule |
Emp. Form. | C21H17ClN2O2 |
Mol. Mass. | 364.825 |
SMILES | Clc1cccc(c1)C#CCCCCC(=O)c1ncc(o1)-c1ccccn1 |
Structure |
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