Bromine in PDB 8bx3: Fragment-Linked Stabilizer For Era - 14-3-3 Interaction (1074372)

The structure of Fragment-Linked Stabilizer For Era - 14-3-3 Interaction (1074372), PDB code: 8bx3 was solved by E.J.Visser, E.M.F.Vandenboorn, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.96 / 1.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.92, 112.508, 62.491, 90, 90, 90
R / Rfree (%)	18.2 / 18.9

The structure of Fragment-Linked Stabilizer For Era - 14-3-3 Interaction (1074372) also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Bromine atom in the Fragment-Linked Stabilizer For Era - 14-3-3 Interaction (1074372) (pdb code 8bx3). 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 Fragment-Linked Stabilizer For Era - 14-3-3 Interaction (1074372), PDB code: 8bx3:

Bromine binding site 1 out of 1 in the Fragment-Linked Stabilizer For Era - 14-3-3 Interaction (1074372)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Fragment-Linked Stabilizer For Era - 14-3-3 Interaction (1074372) within 5.0Å range: probe atom residue distance (Å) B Occ A:Br304 b:24.2 occ:1.00 BR1 A:RZL304 0.0 24.2 1.0 C02 A:RZL304 1.9 18.5 1.0 C03 A:RZL304 2.8 19.4 1.0 H031 A:RZL304 2.9 23.3 1.0 C28 A:RZL304 2.9 22.4 1.0 HE3 A:LYS122 2.9 13.8 1.0 H281 A:RZL304 3.0 26.9 1.0 HD3 A:LYS122 3.0 13.1 1.0 HA A:ILE168 3.2 14.5 1.0 HG23 A:ILE168 3.3 15.0 1.0 HZ1 A:LYS122 3.5 16.1 1.0 CD A:LYS122 3.6 10.9 1.0 CE A:LYS122 3.6 11.5 1.0 HD2 A:LYS122 3.6 13.1 1.0 O A:HOH563 3.7 20.6 1.0 HG12 A:ILE168 3.7 15.7 1.0 HE2 A:PHE119 3.8 18.5 1.0 HD2 A:PHE119 3.8 16.6 1.0 O A:HOH568 3.8 18.7 1.0 HA3 A:GLY171 4.0 12.5 1.0 NZ A:LYS122 4.0 13.4 1.0 HG23 B:VAL595 4.0 19.2 1.0 O A:HOH450 4.1 24.2 1.0 CA A:ILE168 4.1 12.1 1.0 C04 A:RZL304 4.2 21.0 1.0 C27 A:RZL304 4.2 22.9 1.0 CE2 A:PHE119 4.2 15.4 1.0 CD2 A:PHE119 4.2 13.8 1.0 CG2 A:ILE168 4.2 12.4 1.0 HZ3 A:LYS122 4.3 16.1 1.0 O A:ILE168 4.4 11.6 1.0 HE2 A:LYS122 4.4 13.8 1.0 CB A:ILE168 4.5 11.8 1.0 CG1 A:ILE168 4.5 13.1 1.0 C05 A:RZL304 4.7 23.2 1.0 HZ2 A:LYS122 4.7 16.1 1.0 HG22 A:ILE168 4.7 15.0 1.0 O A:PRO167 4.8 11.5 1.0 O A:HOH677 4.8 25.4 1.0 HG21 A:ILE168 4.8 15.0 1.0 HA A:PHE119 4.8 12.1 1.0 C A:ILE168 4.8 10.5 1.0 H A:LEU172 4.8 11.5 1.0 CA A:GLY171 4.9 10.4 1.0 H041 A:RZL304 4.9 25.2 1.0 CG2 B:VAL595 4.9 16.0 1.0 HG13 A:ILE168 4.9 15.7 1.0 H271 A:RZL304 4.9 27.6 1.0 HG21 B:VAL595 5.0 19.2 1.0 H A:GLY171 5.0 12.0 1.0 CG A:LYS122 5.0 9.9 1.0

E.J.Visser, P.Jaishankar, E.Sijbesma, M.A.M.Pennings, E.M.F.Vandenboorn, X.Guillory, R.J.Neitz, J.Morrow, S.Dutta, A.R.Renslo, L.Brunsveld, M.R.Arkin, C.Ottmann. From Tethered to Freestanding Stabilizers of 14-3-3 Protein-Protein Interactions Via Fragment Linking. Angew.Chem.Int.Ed.Engl. 08004 2023.
ISSN: ESSN 1521-3773
PubMed: 37455289
DOI: 10.1002/ANIE.202308004