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

Protein crystallography data

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

Other elements in 8bx3:

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

Magnesium (Mg) 3 atoms

Bromine Binding Sites:

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 8bx3

Go back to Bromine Binding Sites List in 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

Reference:

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
Page generated: Thu Jul 11 04:55:27 2024

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