| Reaction Details |
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 | Report a problem with these data |
| Target | Mitogen-activated protein kinase 14 |
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| Ligand | BDBM50328772 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_673596 (CHEMBL1274709) |
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| IC50 | 66±n/a nM |
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| Citation |  Ahn, YM; Clare, M; Ensinger, CL; Hood, MM; Lord, JW; Lu, WP; Miller, DF; Patt, WC; Smith, BD; Vogeti, L; Kaufman, MD; Petillo, PA; Wise, SC; Abendroth, J; Chun, L; Clark, R; Feese, M; Kim, H; Stewart, L; Flynn, DL Switch control pocket inhibitors of p38-MAP kinase. Durable type II inhibitors that do not require binding into the canonical ATP hinge region. Bioorg Med Chem Lett20:5793-8 (2010) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Mitogen-activated protein kinase 14 |
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| Name: | Mitogen-activated protein kinase 14 |
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| Synonyms: | CSAID-binding protein | CSBP | CSBP1 | CSBP2 | CSPB1 | Cytokine suppressive anti-inflammatory drug-binding protein | MAP kinase 14 | MAP kinase MXI2 | MAP kinase p38 alpha | MAPK 14 | MAPK14 | MAX-interacting protein 2 | MK14_HUMAN | MXI2 | Mitogen-activated protein kinase p38 alpha | SAPK2A | Stress-activated protein kinase 2a | p38 MAP kinase alpha/beta |
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| Type: | Serine/threonine-protein kinase |
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| Mol. Mass.: | 41286.76 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Q16539 |
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| Residue: | 360 |
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| Sequence: | MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQ
SIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQ
KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMT
GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVG
TPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAA
QALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
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| BDBM50328772 |
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| n/a |
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| Name | BDBM50328772 |
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| Synonyms: | 2-(3-(5-(3-(2,3-dichlorophenyl)ureido)-3-(thiophen-2-yl)-1H-pyrazol-1-yl)phenyl)acetamide | CHEMBL1269839 |
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| Type | Small organic molecule |
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| Emp. Form. | C22H17Cl2N5O2S |
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| Mol. Mass. | 486.374 |
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| SMILES | NC(=O)Cc1cccc(c1)-n1nc(cc1NC(=O)Nc1cccc(Cl)c1Cl)-c1cccs1 |
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| Structure | 
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