Reaction Details |
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Target | 72 kDa type IV collagenase |
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Ligand | BDBM50288677 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEBML_101916 |
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Ki | 4.8±n/a nM |
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Citation | Caldwell, CG; Sahoo, SP; Polo, SA; Eversole, RR; Lanza, TJ; Mills, SG; Niedzwiecki, LM; Izquierdo-Martin, M; Chang, BC; Harrison, RK; Kuo, DW; Lin, TY; Stein, RL; Durette, PL; Hagmann, WK Phosphinic acid inhibitors of matrix metalloproteinases Bioorg Med Chem Lett6:323-328 (1996) Article |
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More Info.: | Get all data from this article, Assay Method |
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72 kDa type IV collagenase |
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Name: | 72 kDa type IV collagenase |
Synonyms: | 72 kDa gelatinase | 72 kDa type IV collagenase precursor | CLG4A | Gelatinase A | Gelatinase A (MMP-2) | MMP2 | MMP2_HUMAN | Matrix metalloproteinase-2 | Matrix metalloproteinase-2 (MMP 2) | Matrix metalloproteinase-2 (MMP2) | Matrix metalloproteinases 2 (MMP-2) | TBE-1 |
Type: | Enzyme |
Mol. Mass.: | 73870.36 |
Organism: | Homo sapiens (Human) |
Description: | P08253 |
Residue: | 660 |
Sequence: | MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGC
PKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWD
KNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGD
GYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFN
GKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGT
SYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKY
ESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGAL
MAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQ
IRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEY
WIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDP
GFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
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BDBM50288677 |
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n/a |
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Name | BDBM50288677 |
Synonyms: | CHEMBL324691 | [(E)-4-(1,3-Dioxo-1,3-dihydro-isoindol-2-yl)-but-2-enyl]-[(S)-2-((S)-3-methyl-1-phenylcarbamoyl-butylcarbamoyl)-4-phenyl-butyl]-phosphinic acid |
Type | Small organic molecule |
Emp. Form. | C35H40N3O6P |
Mol. Mass. | 629.6824 |
SMILES | CC(C)C[C@H](NC(=O)C(CCc1ccccc1)=CP(O)(=O)CCCCN1C(=O)c2ccccc2C1=O)C(=O)Nc1ccccc1 |w:17.18| |
Structure |
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