Reaction Details |
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Target | Matrix metalloproteinase-9 |
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Ligand | BDBM50230516 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_461907 (CHEMBL944754) |
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IC50 | 1.3±n/a nM |
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Citation | Yang, SM; Scannevin, RH; Wang, B; Burke, SL; Huang, Z; Karnachi, P; Wilson, LJ; Rhodes, KJ; Lagu, B; Murray, WV beta-N-Biaryl ether sulfonamide hydroxamates as potent gelatinase inhibitors: part 2. Optimization of alpha-amino substituents. Bioorg Med Chem Lett18:1140-5 (2008) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Matrix metalloproteinase-9 |
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Name: | Matrix metalloproteinase-9 |
Synonyms: | 67 kDa matrix metalloproteinase-9 | 82 kDa matrix metalloproteinase-9 | 92 kDa gelatinase | 92 kDa type IV collagenase | CLG4B | GELB | Gelatinase B | MMP-9 | MMP9 | MMP9_HUMAN | Matrix metalloproteinase 9 (MMP-9) | Matrix metalloproteinase-9 (MMP-9) | Matrix metalloproteinase-9 (MMP9) |
Type: | Enzyme |
Mol. Mass.: | 78452.28 |
Organism: | Homo sapiens (Human) |
Description: | P14780 |
Residue: | 707 |
Sequence: | MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEM
RGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHN
ITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYP
FDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRS
YSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYS
ACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYST
CTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMY
PMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSER
PTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYW
RFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRR
LDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLD
THDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED
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BDBM50230516 |
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n/a |
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Name | BDBM50230516 |
Synonyms: | (S)-2-(4-fluorophenylamino)-N-hydroxy-3-(N-(4-(p-tolyloxy)phenyl)methan-2-ylsulfonamido)propanamide | CHEMBL399565 |
Type | Small organic molecule |
Emp. Form. | C23H24FN3O5S |
Mol. Mass. | 473.517 |
SMILES | Cc1ccc(Oc2ccc(cc2)N(C[C@H](Nc2ccc(F)cc2)C(=O)NO)S(C)(=O)=O)cc1 |
Structure |
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