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TargetMatrix metalloproteinase-9
LigandBDBM50128605
Substrate/Competitorn/a
Meas. Tech.ChEMBL_825929 (CHEMBL2044953)
IC50 11±n/a nM
Citation Zhong, HWees, MAFaure, TDCarrillo, CArbiser, JBowen, JP The impact of ionization States of matrix metalloproteinase inhibitors on docking-based inhibitor design. ACS Med Chem Lett2:455-460 (2011) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
Matrix metalloproteinase-9
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
Blast this sequence in BindingDB or PDB
  Blast E-value cutoff:
BDBM50128605
n/a
NameBDBM50128605
Synonyms:(R)-3-(4-(2-(diethylamino)ethoxy)phenyl)-2-(4-ethoxyphenylsulfonyl)-N-hydroxy-2-methylpropanamide | 3-[4-(2-Diethylamino-ethoxy)-phenyl]-2-(4-ethoxy-benzenesulfonyl)-N-hydroxy-2-methyl-propionamide | CHEMBL310338
TypeSmall organic molecule
Emp. Form.C24H34N2O6S
Mol. Mass.478.602
SMILESCCOc1ccc(cc1)S(=O)(=O)C(C)(Cc1ccc(OCCN(CC)CC)cc1)C(=O)NO
Structure
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