Reaction Details |
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Target | Solute carrier family 15 member 1 |
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Ligand | BDBM50370586 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_302952 (CHEMBL841787) |
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Ki | 340000±n/a nM |
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Citation | Biegel, A; Gebauer, S; Hartrodt, B; Brandsch, M; Neubert, K; Thondorf, I Three-dimensional quantitative structure-activity relationship analyses of beta-lactam antibiotics and tripeptides as substrates of the mammalian H+/peptide cotransporter PEPT1. J Med Chem48:4410-9 (2005) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Solute carrier family 15 member 1 |
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Name: | Solute carrier family 15 member 1 |
Synonyms: | Intestinal H(+)/peptide cotransporter | Oligopeptide transporter small intestine isoform | Oligopeptide transporter, small intestine isoform | PEPT1 | Peptide transporter 1 | S15A1_HUMAN | SLC15A1 |
Type: | PROTEIN |
Mol. Mass.: | 78818.07 |
Organism: | Homo sapiens (Human) |
Description: | ChEMBL_1488839 |
Residue: | 708 |
Sequence: | MGMSKSHSFFGYPLSIFFIVVNEFCERFSYYGMRAILILYFTNFISWDDNLSTAIYHTFV
ALCYLTPILGALIADSWLGKFKTIVSLSIVYTIGQAVTSVSSINDLTDHNHDGTPDSLPV
HVVLSLIGLALIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLLSTII
TPMLRVQQCGIHSKQACYPLAFGVPAALMAVALIVFVLGSGMYKKFKPQGNIMGKVAKCI
GFAIKNRFRHRSKAFPKREHWLDWAKEKYDERLISQIKMVTRVMFLYIPLPMFWALFDQQ
GSRWTLQATTMSGKIGALEIQPDQMQTVNAILIVIMVPIFDAVLYPLIAKCGFNFTSLKK
MAVGMVLASMAFVVAAIVQVEIDKTLPVFPKGNEVQIKVLNIGNNTMNISLPGEMVTLGP
MSQTNAFMTFDVNKLTRINISSPGSPVTAVTDDFKQGQRHTLLVWAPNHYQVVKDGLNQK
PEKGENGIRFVNTFNELITITMSGKVYANISSYNASTYQFFPSGIKGFTISSTEIPPQCQ
PNFNTFYLEFGSAYTYIVQRKNDSCPEVKVFEDISANTVNMALQIPQYFLLTCGEVVFSV
TGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGQFSKQWAEYILFAALLLVVC
VIFAIMARFYTYINPAEIEAQFDEDEKKNRLEKSNPYFMSGANSQKQM
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BDBM50370586 |
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n/a |
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Name | BDBM50370586 |
Synonyms: | 7-(2-(2-amino-4-thiazolyl)-4-carboxy-2-butenoylamino)-3-cephem-4-carboxylic acid | 7432-S | CEFTIBUTEN | Cedax | Cedex | SCH-39720 |
Type | Small organic molecule |
Emp. Form. | C15H14N4O6S2 |
Mol. Mass. | 410.425 |
SMILES | Nc1nc(cs1)C(=C\CC(O)=O)\C(=O)N[C@H]1[C@H]2SCC=C(N2C1=O)C(O)=O |r,c:20| |
Structure |
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