Bromine in PDB 4tqb: The Co-Complex Structure of the Translation Initiation Factor EIF4E with the Inhibitor 4EGI-1 Reveals An Allosteric Mechanism For Dissociating EIF4G

The structure of The Co-Complex Structure of the Translation Initiation Factor EIF4E with the Inhibitor 4EGI-1 Reveals An Allosteric Mechanism For Dissociating EIF4G, PDB code: 4tqb was solved by E.Papadopoulos, S.Jenni, G.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.39 / 1.59
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.830, 73.480, 66.260, 90.00, 106.66, 90.00
R / Rfree (%)	18.2 / 21.1

The binding sites of Bromine atom in the The Co-Complex Structure of the Translation Initiation Factor EIF4E with the Inhibitor 4EGI-1 Reveals An Allosteric Mechanism For Dissociating EIF4G (pdb code 4tqb). 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 The Co-Complex Structure of the Translation Initiation Factor EIF4E with the Inhibitor 4EGI-1 Reveals An Allosteric Mechanism For Dissociating EIF4G, PDB code: 4tqb:

Bromine binding site 1 out of 1 in the The Co-Complex Structure of the Translation Initiation Factor EIF4E with the Inhibitor 4EGI-1 Reveals An Allosteric Mechanism For Dissociating EIF4G


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of The Co-Complex Structure of the Translation Initiation Factor EIF4E with the Inhibitor 4EGI-1 Reveals An Allosteric Mechanism For Dissociating EIF4G within 5.0Å range: probe atom residue distance (Å) B Occ A:Br302 b:37.0 occ:1.00 BR1 A:34K302 0.0 37.0 1.0 C18 A:34K302 1.9 36.6 1.0 HG22 A:ILE79 2.8 19.5 0.6 C20 A:34K302 2.9 36.4 1.0 C17 A:34K302 2.9 36.5 1.0 H201 A:34K302 2.9 43.7 1.0 H171 A:34K302 3.0 43.8 1.0 HG21 A:ILE63 3.0 25.6 1.0 HG21 A:ILE79 3.1 19.5 0.6 HD2 A:HIS78 3.3 22.7 1.0 CG2 A:ILE79 3.4 16.2 0.6 HG23 A:ILE63 3.4 25.6 1.0 HD11 A:LEU75 3.5 15.8 1.0 CG2 A:ILE63 3.6 21.3 1.0 HD11 A:ILE79 3.7 18.8 0.5 HE2 A:HIS78 3.7 26.2 1.0 HD13 A:ILE63 3.8 21.3 1.0 HD12 A:LEU75 3.8 15.8 1.0 HG12 A:ILE79 3.8 19.2 0.5 HG23 A:ILE79 3.8 19.5 0.6 HG22 A:ILE63 3.9 25.6 1.0 CD2 A:HIS78 4.0 18.9 1.0 O A:HOH454 4.0 27.5 1.0 CD1 A:LEU75 4.0 13.2 1.0 HG13 A:ILE79 4.1 19.2 0.5 O A:HOH433 4.1 37.2 1.0 C21 A:34K302 4.2 36.1 1.0 NE2 A:HIS78 4.2 21.9 1.0 C16 A:34K302 4.2 36.2 1.0 HD13 A:LEU75 4.3 15.8 1.0 CG1 A:ILE79 4.3 16.0 0.5 CD1 A:ILE79 4.4 15.7 0.5 HB A:ILE79 4.6 19.4 0.6 CB A:ILE79 4.6 16.2 0.6 HD23 A:LEU45 4.7 14.5 1.0 C15 A:34K302 4.7 36.0 1.0 CD1 A:ILE63 4.7 17.8 1.0 HG12 A:ILE63 4.9 18.7 1.0 HD13 A:ILE79 4.9 18.8 0.5 H211 A:34K302 4.9 43.3 1.0 H161 A:34K302 4.9 43.5 1.0 CB A:ILE63 4.9 18.6 1.0

E.Papadopoulos, S.Jenni, E.Kabha, K.J.Takrouri, T.Yi, N.Salvi, R.E.Luna, E.Gavathiotis, P.Mahalingam, H.Arthanari, R.Rodriguez-Mias, R.Yefidoff-Freedman, B.H.Aktas, M.Chorev, J.A.Halperin, G.Wagner. Structure of the Eukaryotic Translation Initiation Factor EIF4E in Complex with 4EGI-1 Reveals An Allosteric Mechanism For Dissociating EIF4G. Proc.Natl.Acad.Sci.Usa V. 111 E3187 2014.
ISSN: ESSN 1091-6490
PubMed: 25049413
DOI: 10.1073/PNAS.1410250111