3VBQ

Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in Pim-1 kinase needle screening and inhibitor design

Summary for 3VBQ

• Entry DOI: 10.2210/pdb3vbq/pdb
• Related: 3VBT 3VBV 3VBW 3VBX 3VBY 3VC4
• Descriptor: Serine/threonine-protein kinase pim-1, (5~{Z})-5-[[3-[6-[(4-azanylcyclohexyl)amino]pyrazin-2-yl]phenyl]methylidene]-1,3-thiazolidine-2,4-dione (3 entities in total)
• Functional Keywords: pim1, rossmann fold, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 34876.57

Authors

Liu, J. (deposition date: 2012-01-02, release date: 2012-03-21, Last modification date: 2024-02-28)

• Primary citation: Good, A.C.,Liu, J.,Hirth, B.,Asmussen, G.,Xiang, Y.,Biemann, H.P.,Bishop, K.A.,Fremgen, T.,Fitzgerald, M.,Gladysheva, T.,Jain, A.,Jancsics, K.,Metz, M.,Papoulis, A.,Skerlj, R.,Stepp, J.D.,Wei, R.R.; Implications of promiscuous Pim-1 kinase fragment inhibitor hydrophobic interactions for fragment-based drug design.; J.Med.Chem., 55:2641-2648, 2012; PubMed: 22339127; DOI: 10.1021/jm2014698

Experimental method

X-RAY DIFFRACTION (1.85 Å)