Reaction Details |
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Target | Protein RecA |
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Ligand | BDBM70428 |
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Substrate/Competitor | n/a |
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Meas. Tech. | Fluorescence Cell-Free Homogeneous Dose Retest to Identify Inhibitors of RecA-Intein Splicing Activity |
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EC50 | 26300±n/a nM |
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Citation | PubChem, PC Fluorescence Cell-Free Homogeneous Dose Retest to Identify Inhibitors of RecA-Intein Splicing Activity PubChem Bioassay(2010)[AID] |
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More Info.: | Get all data from this article, Solution Info, Assay Method |
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Protein RecA |
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Name: | Protein RecA |
Synonyms: | DNA recombination protein RecA | RECA_MYCTU | recA |
Type: | Enzyme Catalytic Domain |
Mol. Mass.: | 85386.52 |
Organism: | Mycobacterium tuberculosis H37Rv |
Description: | gi_15609874 |
Residue: | 790 |
Sequence: | MTQTPDREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRG
RVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQP
DTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMT
GALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVG
NRTRVKVVKNKCLAEGTRIFDPVTGTTHRIEDVVDGRKPIHVVAAAKDGTLHARPVVSWF
DQGTRDVIGLRIAGGAIVWATPDHKVLTEYGWRAAGELRKGDRVAQPRRFDGFGDSAPIP
ADHARLLGYLIGDGRDGWVGGKTPINFINVQRALIDDVTRIAATLGCAAHPQGRISLAIA
HRPGERNGVADLCQQAGIYGKLAWEKTIPNWFFEPDIAADIVGNLLFGLFESDGWVSREQ
TGALRVGYTTTSEQLAHQIHWLLLRFGVGSTVRDYDPTQKRPSIVNGRRIQSKRQVFEVR
ISGMDNVTAFAESVPMWGPRGAALIQAIPEATQGRRRGSQATYLAAEMTDAVLNYLDERG
VTAQEAAAMIGVASGDPRGGMKQVLGASRLRRDRVQALADALDDKFLHDMLAEELRYSVI
REVLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGV
DQGLIRKSGAWFTYEGEQLGQGKENARNFLVENADVADEIEKKIKEKLGIGAVVTDDPSN
DGVLPAPVDF
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BDBM70428 |
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n/a |
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Name | BDBM70428 |
Synonyms: | 3-chloranyl-1-(2,5-dimethoxyphenyl)-4-morpholin-4-yl-pyrrole-2,5-dione | 3-chloro-1-(2,5-dimethoxyphenyl)-4-(4-morpholinyl)pyrrole-2,5-dione | 3-chloro-1-(2,5-dimethoxyphenyl)-4-morpholin-4-ylpyrrole-2,5-dione | 3-chloro-1-(2,5-dimethoxyphenyl)-4-morpholino-3-pyrroline-2,5-quinone | MLS000106275 | SMR000103244 | cid_1379075 |
Type | Small organic molecule |
Emp. Form. | C16H17ClN2O5 |
Mol. Mass. | 352.77 |
SMILES | COc1ccc(OC)c(c1)N1C(=O)C(Cl)=C(N2CCOCC2)C1=O |t:15| |
Structure |
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