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Bromine in PDB 3vbx: Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design

Enzymatic 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:

Resolution Low / High (Å) 84.00 / 2.03
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 97.000, 97.000, 81.000, 90.00, 90.00, 120.00
R / Rfree (%) 21.8 / 25.8

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 3vbx

Go back to Bromine Binding Sites List in 3vbx
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

A full contact list of Bromine with other atoms in the Br binding site number 1 of Exploitation of Hydrogen Bonding Constraints and Flat Hydrophobic Energy Landscapes in Pim-1 Kinase Needle Screening and Inhibitor Design within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1

b:52.4
occ:1.00
BR1 A:0FO1 0.0 52.4 1.0
CAJ A:0FO1 1.8 32.3 1.0
CAK A:0FO1 2.7 33.6 1.0
CAI A:0FO1 2.7 35.6 1.0
CD1 A:LEU44 3.7 32.1 1.0
CG A:ARG122 3.8 31.0 1.0
CAL A:0FO1 4.0 29.1 1.0
CAB A:0FO1 4.0 33.7 1.0
CD1 A:LEU174 4.0 27.4 1.0
O A:HOH368 4.0 36.0 1.0
CG1 A:VAL126 4.0 28.7 1.0
CD A:ARG122 4.1 33.6 1.0
CAA A:0FO1 4.4 31.3 1.0
CB A:ARG122 4.5 33.8 1.0
CB A:ALA65 4.6 27.0 1.0
CG2 A:VAL126 4.7 28.7 1.0
CA A:ARG122 4.9 31.9 1.0
CB A:VAL126 4.9 31.6 1.0
CD2 A:LEU174 5.0 23.2 1.0

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.
ISSN: ISSN 0022-2623
PubMed: 22339127
DOI: 10.1021/JM2014698
Page generated: Sat Dec 12 02:16:40 2020

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