Reaction Details |
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Target | 11-beta-hydroxysteroid dehydrogenase type 2 |
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Ligand | BDBM50339812 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_735656 (CHEMBL1693471) |
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IC50 | 17±n/a nM |
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Citation | Gaware, R; Khunt, R; Czollner, L; Stanetty, C; Da Cunha, T; Kratschmar, DV; Odermatt, A; Kosma, P; Jordis, U; Classen-Houben, D Synthesis of new glycyrrhetinic acid derived ring A azepanone, 29-urea and 29-hydroxamic acid derivatives as selective 11ß-hydroxysteroid dehydrogenase 2 inhibitors. Bioorg Med Chem19:1866-80 (2011) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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11-beta-hydroxysteroid dehydrogenase type 2 |
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Name: | 11-beta-hydroxysteroid dehydrogenase type 2 |
Synonyms: | 11-DH2 | 11-beta-HSD2 | 11-beta-Hydroxysteroid Dehydrogenase 2 (11-beta-HSD2) | 11-beta-hydroxysteroid dehydrogenase | 11-beta-hydroxysteroid dehydrogenase 2 | 11-beta-hydroxysteroid dehydrogenase type 2 | 11-beta-hydroxysteroid dehydrogenase type 2 (11-beta-HSD2) | Corticosteroid 11-beta-dehydrogenase isozyme 2 | DHI2_HUMAN | HSD11B2 | HSD11K | NAD-dependent 11-beta-hydroxysteroid dehydrogenase | SDR9C3 |
Type: | Enzyme |
Mol. Mass.: | 44141.72 |
Organism: | Homo sapiens (Human) |
Description: | Purified recombinant human 11beta-HSD2. |
Residue: | 405 |
Sequence: | MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAV
LAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPG
AIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELS
PVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVA
LLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYI
EHLHGQFLHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMYFIHYYLPEGLRR
RFLQAFFISHCLPRALQPGQPGTTPPQDAAQDPNLSPGPSPAVAR
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BDBM50339812 |
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n/a |
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Name | BDBM50339812 |
Synonyms: | CHEMBL1689283 | N-[(3beta,18beta,20beta)-3-Hydroxy-11-oxo-30-norolean-12-en-20-yl]urea |
Type | Small organic molecule |
Emp. Form. | C30H48N2O3 |
Mol. Mass. | 484.7137 |
SMILES | CC1(C)[C@@H](O)CC[C@@]2(C)[C@H]1CC[C@]1(C)[C@@H]2C(=O)C=C2[C@@H]3C[C@](C)(CC[C@]3(C)CC[C@@]12C)NC(N)=O |r,t:19| |
Structure |
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