Reaction Details |
| Report a problem with these data |
Target | Peptidase |
---|
Ligand | BDBM50378857 |
---|
Substrate/Competitor | n/a |
---|
Meas. Tech. | ChEMBL_705367 (CHEMBL1662792) |
---|
pH | 7.4±n/a |
---|
IC50 | 1900±n/a nM |
---|
Comments | extracted |
---|
Citation | Lemaire, S; Glupczynski, Y; Duval, V; Joris, B; Tulkens, PM; Van Bambeke, F Activities of ceftobiprole and other cephalosporins against extracellular and intracellular (THP-1 macrophages and keratinocytes) forms of methicillin-susceptible and methicillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother53:2289-97 (2009) [PubMed] Article |
---|
More Info.: | Get all data from this article, Assay Method |
---|
|
Peptidase |
---|
Name: | Peptidase |
Synonyms: | MecA | Pbp2a | Penicillin binding protein 2 prime | Penicillin binding protein 2' | Penicillin binding protein 2a (PBP2a) | Penicillin-binding protein 2 prime | Penicillin-binding protein 2' |
Type: | PROTEIN |
Mol. Mass.: | 76113.18 |
Organism: | Staphylococcus aureus |
Description: | ChEMBL_677175 |
Residue: | 668 |
Sequence: | MKKIKIVPLILIVVVVGFGIYFYASKDKEINNTIDAIEDKNFKQVYKDSSYISKSDNGEV
EMTERPIKIYNSLGVKDINIQDRKIKKVSKNKKRVDAQYKIKTNYGNIDRNVQFNFVKED
GMWKLDWDHSVIIPGMQKDQSIHIENLKSERGKILDRNNVELANTGTAYEIGIVPKNVSK
KDYKAIAKELSISEDYIKQQMDQNWVQDDTFVPLKTVKKMDEYLSDFAKKFHLTTNETES
RNYPLGKATSHLLGYVGPINSEELKQKEYKGYKDDAVIGKKGLEKLYDKKLQHEDGYRVT
IVDDNSNTIAHTLIEKKKKDGKDIQLTIDAKVQKSIYNNMKNDYGSGTAIHPQTGELLAL
VSTPSYDVYPFMYGMSNEEYNKLTEDKKEPLLNKFQITTSPGSTQKILTAMIGLNNKTLD
DKTSYKIDGKGWQKDKSWGGYNVTRYEVVNGNIDLKQAIESSDNIFFARVALELGSKKFE
KGMKKLGVGEDIPSDYPFYNAQISNKNLDNEILLADSGYGQGEILINPVQILSIYSALEN
NGNINAPHLLKDTKNKVWKKNIISKENINLLTDGMQQVVNKTHKEDIYRSYANLIGKSGT
AELKMKQGETGRQIGWFISYDKDNPNMMMAINVKDVQDKGMASYNAKISGKVYDELYENG
NKKYDIDE
|
|
|
BDBM50378857 |
---|
n/a |
---|
Name | BDBM50378857 |
Synonyms: | CEFTOBIPROLE | Zeftera | Zevtera |
Type | Small organic molecule |
Emp. Form. | C20H22N8O6S2 |
Mol. Mass. | 534.569 |
SMILES | Nc1nc(ns1)C(N=O)C(=O)N[C@H]1[C@H]2SCC(C=C3CCN([C@@H]4CCNC4)C3=O)=C(N2C1=O)C(O)=O |r,w:17.17,c:31| |
Structure |
|