| Reaction Details |
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 | Report a problem with these data |
| Target | Penicillin-binding protein 1A |
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| Ligand | BDBM50103601 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_672067 (CHEMBL1267448) |
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| IC50 | 180±n/a nM |
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| Citation |  Kosowska-Shick, K; McGhee, PL; Appelbaum, PC Affinity of ceftaroline and other beta-lactams for penicillin-binding proteins from Staphylococcus aureus and Streptococcus pneumoniae. Antimicrob Agents Chemother54:1670-7 (2010) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Penicillin-binding protein 1A |
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| Name: | Penicillin-binding protein 1A |
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| Synonyms: | 2.4.1.129 | 3.4.16.4 | DD-transpeptidase | PBP-1A | PBPA_STRPN | Penicillin-binding protein 1A | Penicillin-insensitive transglycosylase | Penicillin-sensitive transpeptidase | Peptidoglycan TGase | ponA |
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| Type: | PROTEIN |
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| Mol. Mass.: | 79749.99 |
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| Organism: | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
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| Description: | ChEMBL_103552 |
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| Residue: | 719 |
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| Sequence: | MNKPTILRLIKYLSISFLSLVIAAIVLGGGVFFYYVSKAPSLSESKLVATTSSKIYDNKN
QLIADLGSERRVNAQANDIPTDLVKAIVSIEDHRFFDHRGIDTIRILGAFLRNLQSNSLQ
GGSTLTQQLIKLTYFSTSTSDQTISRKAQEAWLAIQLEQKATKQEILTYYINKVYMSNGN
YGMQTAAQNYYGKDLNNLSLPQLALLAGMPQAPNQYDPYSHPEAAQDRRNLVLSEMKNQG
YISAEQYEKAVNTPITDGLQSLKSASNYPAYMDNYLKEVINQVEEETGYNLLTTGMDVYT
NVDQEAQKHLWDIYNTDEYVAYPDDELQVASTIVDVSNGKVIAQLGARHQSSNVSFGINQ
AVETNRDWGSTMKPITDYAPALEYGVYDSTATIVHDEPYNYPGTNTPVYNWDRGYFGNIT
LQYALQQSRNVPAVETLNKVGLNRAKTFLNGLGIDYPSIHYSNAISSNTTESDKKYGASS
EKMAAAYAAFANGGTYYKPMYIHKVVFSDGSEKEFSNVGTRAMKETTAYMMTDMMKTVLT
YGTGRNAYLAWLPQAGKTGTSNYTDEEIENHIKTSQFVAPDELFAGYTRKYSMAVWTGYS
NRLTPLVGNGLTVAAKVYRSMMTYLSEGSNPEDWNIPEGLYRNGEFVFKNGARSTWNSPA
PQQPPSTESSSSSSDSSTSQSSSTTPSTNNSTTTNPNNNTQQSNTTPDQQNQNPQPAQP
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| BDBM50103601 |
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| n/a |
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| Name | BDBM50103601 |
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| Synonyms: | CHEBI:29007 | Ceftriaxone |
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| Type | Small organic molecule |
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| Emp. Form. | C18H18N8O7S3 |
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| Mol. Mass. | 554.58 |
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| SMILES | [H][C@@]1(NC(=O)C(=N/OC)\c2csc(N)n2)C(=O)N2C(C(O)=O)=C(CSc3nc(=O)c(O)nn3C)CS[C@]12[H] |t:22| |
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| Structure | 
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