4GG5
Crystal structure of CMET in complex with novel inhibitor
Summary for 4GG5
| Entry DOI | 10.2210/pdb4gg5/pdb |
| Related | 4GG7 |
| Descriptor | Hepatocyte growth factor receptor, 3-(4-methylpiperazin-1-yl)-N-(3-nitrobenzyl)-7-(trifluoromethyl)quinolin-5-amine (3 entities in total) |
| Functional Keywords | cmet inhibitor, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein. Isoform 3: Secreted: P08581 |
| Total number of polymer chains | 1 |
| Total formula weight | 36479.03 |
| Authors | Liu, Q.F.,Chen, T.T.,Xu, Y.C. (deposition date: 2012-08-05, release date: 2012-10-03, Last modification date: 2024-02-28) |
| Primary citation | Wu, K.,Ai, J.,Liu, Q.,Chen, T.,Zhao, A.,Peng, X.,Wang, Y.,Ji, Y.,Yao, Q.,Xu, Y.,Geng, M.,Zhang, A. Multisubstituted quinoxalines and pyrido[2,3-d]pyrimidines: Synthesis and SAR study as tyrosine kinase c-Met inhibitors. Bioorg.Med.Chem.Lett., 22:6368-6372, 2012 Cited by PubMed Abstract: Two series of new analogues were designed by replacing the quinoline scaffold of our earlier lead 2 (zgw-atinib) with quinoxaline and pyrido[2,3-d]pyrimidine frameworks. Moderate c-Met inhibitory activity was observed in the quinoxaline series. Among the pyrido[2,3-d]pyrimidine series, compounds 13a-c possessing an O-linkage were inactive, whilst the N-linked analogues 15a-c retained c-Met inhibitory potency. Highest activity was observed in the 3-nitrobenzyl analog 15b that showed an IC(50) value of 6.5 nM. Further structural modifications based on this compound were undergoing. PubMed: 22985853DOI: 10.1016/j.bmcl.2012.08.075 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.423 Å) |
Structure validation
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