| Reaction Details |
|---|
 | Report a problem with these data |
| Target | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
|---|
| Ligand | BDBM50478376 |
|---|
| Substrate/Competitor | n/a |
|---|
| Meas. Tech. | ChEMBL_809999 (CHEMBL2015108) |
|---|
| Ki | 20±n/a nM |
|---|
| Citation |  Warmus, JS; Quinn, CL; Taylor, C; Murphy, ST; Johnson, TA; Limberakis, C; Ortwine, D; Bronstein, J; Pagano, P; Knafels, JD; Lightle, S; Mochalkin, I; Brideau, R; Podoll, T Structure based design of an in vivo active hydroxamic acid inhibitor of P. aeruginosa LpxC. Bioorg Med Chem Lett22:2536-43 (2012) [PubMed] Article |
|---|
| More Info.: | Get all data from this article, Assay Method |
|---|
| |
| UDP-3-O-acyl-N-acetylglucosamine deacetylase |
|---|
| Name: | UDP-3-O-acyl-N-acetylglucosamine deacetylase |
|---|
| Synonyms: | LPXC_ECOLI | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (LpxC) | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (LxpC) | UDP-3-O-acyl-GlcNAc deacetylase | asmB | envA | lpxC |
|---|
| Type: | Enzyme |
|---|
| Mol. Mass.: | 33952.00 |
|---|
| Organism: | Escherichia coli |
|---|
| Description: | P0A725 |
|---|
| Residue: | 305 |
|---|
| Sequence: | MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDT
MLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGI
DELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSAD
AFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKM
LDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAP
SAVLA
|
|
|
|---|
| BDBM50478376 |
|---|
| n/a |
|---|
| Name | BDBM50478376 |
|---|
| Synonyms: | BB-78485 | CHEMBL261713 |
|---|
| Type | Small organic molecule |
|---|
| Emp. Form. | C23H20N2O4S |
|---|
| Mol. Mass. | 420.481 |
|---|
| SMILES | ONC(=O)[C@@H](Cc1ccc2ccccc2c1)NS(=O)(=O)c1ccc2ccccc2c1 |r| |
|---|
| Structure | 
|
|---|
Search and Browse
