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Atomistry » Bromine » PDB 3u2d-3wk9 » 3vbx » |
Bromine in PDB 3vbx: Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor DesignEnzymatic activity of Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design
All present enzymatic activity of Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design:
2.7.11.1; Protein crystallography data
The structure of Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design, PDB code: 3vbx
was solved by
J.Liu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Bromine Binding Sites:
The binding sites of Bromine atom in the Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design
(pdb code 3vbx). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design, PDB code: 3vbx: Bromine binding site 1 out of 1 in 3vbxGo back to![]() ![]()
Bromine binding site 1 out
of 1 in the Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design
![]() Mono view ![]() Stereo pair view
Reference:
A.C.Good,
J.Liu,
B.Hirth,
G.Asmussen,
Y.Xiang,
H.P.Biemann,
K.A.Bishop,
T.Fremgen,
M.Fitzgerald,
T.Gladysheva,
A.Jain,
K.Jancsics,
M.Metz,
A.Papoulis,
R.Skerlj,
J.D.Stepp,
R.R.Wei.
Implications of Promiscuous Pim-1 Kinase Fragment Inhibitor Hydrophobic Interactions For Fragment-Based Drug Design. J.Med.Chem. V. 55 2641 2012.
Page generated: Mon Jul 7 06:07:16 2025
ISSN: ISSN 0022-2623 PubMed: 22339127 DOI: 10.1021/JM2014698 |
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