Bromine in PDB 7nqp: 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound LVD1009

The structure of 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound LVD1009, PDB code: 7nqp was solved by M.Wolter, L.V.Dijck, P.J.Cossar, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.38 / 1.24
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.408, 112.028, 62.602, 90, 90, 90
R / Rfree (%)	19.5 / 21.7

The structure of 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound LVD1009 also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Bromine atom in the 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound LVD1009 (pdb code 7nqp). 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 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound LVD1009, PDB code: 7nqp:

Bromine binding site 1 out of 1 in the 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound LVD1009


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of 14-3-3 Sigma with Rela/P65 Binding Site PS45 and Covalently Bound LVD1009 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br301 b:30.0 occ:1.00 BR5 A:TJ8301 0.0 30.0 1.0 C04 A:TJ8301 2.0 25.4 1.0 C03 A:TJ8301 2.9 21.7 1.0 C06 A:TJ8301 2.9 29.6 1.0 O A:HOH553 3.0 36.8 1.0 C02 A:TJ8301 3.1 17.1 1.0 OG A:SER45 3.3 16.3 1.0 O P:HOH103 3.5 21.9 1.0 CE2 A:PHE119 3.8 15.0 1.0 CZ A:PHE119 3.8 14.3 1.0 O A:HOH541 4.0 17.9 1.0 CB A:SER45 4.0 13.7 1.0 C09 A:TJ8301 4.2 31.3 1.0 C07 A:TJ8301 4.2 22.8 1.0 NZ A:LYS122 4.5 16.4 1.0 OD1 A:ASN42 4.5 23.6 1.0 C08 A:TJ8301 4.8 27.9 1.0 CD2 A:PHE119 4.8 15.7 1.0 CE1 A:PHE119 4.8 13.6 1.0 CG2 P:ILE46 5.0 21.4 1.0

P.J.Cossar, M.Wolter, L.Van Dijck, D.Valenti, L.M.Levy, C.Ottmann, L.Brunsveld. Reversible Covalent Imine-Tethering For Selective Stabilization of 14-3-3 Hub Protein Interactions. J.Am.Chem.Soc. 2021.
ISSN: ESSN 1520-5126
PubMed: 34047554
DOI: 10.1021/JACS.1C03035