3VBY

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

Summary for 3VBY

• Entry DOI: 10.2210/pdb3vby/pdb
• Related: 3VBQ 3VBT 3VBV 3VBW 3VBX 3VC4
• Descriptor: Serine/threonine-protein kinase pim-1, furan-2-yl(1H-indol-3-yl)methanone, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: pim1, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 2: Cytoplasm. Isoform 1: Cell membrane: P11309
• Total number of polymer chains: 1
• Total formula weight: 34830.48

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 (2.27 Å)