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Bromine in PDB 8pot: Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation

Enzymatic activity of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation

All present enzymatic activity of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation:
6.1.1.4;

Protein crystallography data

The structure of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation, PDB code: 8pot was solved by A.Palencia, G.Hoffmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.06 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 89.167, 76.794, 90.863, 90, 102.55, 90
R / Rfree (%) 21.4 / 26.5

Bromine Binding Sites:

The binding sites of Bromine atom in the Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation (pdb code 8pot). 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 Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation, PDB code: 8pot:

Bromine binding site 1 out of 1 in 8pot

Go back to Bromine Binding Sites List in 8pot
Bromine binding site 1 out of 1 in the Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Ternary Complex of E. Coli Leucyl-Trna Synthetase, Trna(Leu) and the Benzoxaborole CMPD9 in the Editing Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br101

b:39.7
occ:1.00
 BR B:7RZ101 0.0 39.7 1.0
C13 B:7RZ101 1.9 39.7 1.0
C14 B:7RZ101 2.8 39.4 1.0
C11 B:7RZ101 2.9 39.5 1.0
C10 B:7RZ101 3.3 39.0 1.0
OG1 A:THR252 3.3 39.1 1.0
C17 B:7RZ101 3.5 38.4 1.0
CB A:VAL338 3.8 32.5 1.0
C A:HIS341 3.8 35.2 1.0
CB A:ARG249 3.9 35.8 1.0
O A:HIS341 3.9 34.8 1.0
CB A:HIS341 3.9 37.0 1.0
CG2 A:THR252 3.9 37.5 1.0
CB A:THR252 4.0 38.1 1.0
CB A:ASP342 4.1 37.6 1.0
CG1 A:VAL338 4.1 32.7 1.0
C15 B:7RZ101 4.1 39.8 1.0
N A:ASP342 4.1 35.4 1.0
C12 B:7RZ101 4.2 39.3 1.0
CG A:ARG249 4.2 37.0 1.0
CG2 A:VAL338 4.3 32.5 1.0
CA A:HIS341 4.4 35.6 1.0
N18 B:7RZ101 4.4 38.0 1.0
O A:VAL338 4.5 33.9 1.0
CA A:ASP342 4.5 35.8 1.0
NH1 A:ARG249 4.6 44.8 1.0
C16 B:7RZ101 4.7 40.7 1.0
O1 B:7RZ101 4.7 38.6 1.0
CZ A:ARG249 4.7 44.3 1.0
O A:ARG249 4.8 37.1 1.0
CA A:VAL338 5.0 32.8 1.0

Reference:

A.Palencia, G.Hoffmann, M.Lukarska, R.Clare, S.Ward, M.A.Taylor, M.Ringkjobing Jensen. Targeting A Microbiota Wolbachian Aminoacyl-Trna Synthetase to Block Its Pathogenic Host Science Advances 2024.
Page generated: Mon Jul 7 12:30:17 2025

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