Bromine in PDB 7wpi: Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor

Enzymatic activity of Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor

All present enzymatic activity of Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor:
6.1.1.10;

Protein crystallography data

The structure of Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor, PDB code: 7wpi was solved by J.Yi, Z.Cai, H.Qiu, F.Lu, B.Chen, Z.Luo, Q.Gu, J.Xu, H.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.40 / 1.92
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.492, 80.331, 117.961, 90, 90, 90
R / Rfree (%) 21.1 / 23.7

Bromine Binding Sites:

The binding sites of Bromine atom in the Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor (pdb code 7wpi). 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 Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor, PDB code: 7wpi:

Bromine binding site 1 out of 1 in 7wpi

Go back to Bromine Binding Sites List in 7wpi
Bromine binding site 1 out of 1 in the Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br601

b:30.7
occ:1.00
 BR A:1V7601 0.0 30.7 1.0
C11 A:1V7601 1.9 27.6 1.0
C12 A:1V7601 2.8 27.7 1.0
C10 A:1V7601 2.8 27.0 1.0
O1 A:1V7601 3.0 26.4 1.0
O A:VAL234 3.3 23.9 1.0
N A:VAL236 3.7 25.1 1.0
O A:HOH714 3.7 21.7 1.0
C A:TYR235 3.7 25.0 1.0
CA A:TYR235 3.9 25.0 1.0
CZ A:PHE220 4.0 29.4 1.0
CB A:HIS53 4.0 25.0 1.0
CA A:VAL236 4.1 24.9 1.0
N A:GLY54 4.1 25.7 1.0
C13 A:1V7601 4.1 27.4 1.0
C9 A:1V7601 4.1 27.1 1.0
OD2 A:ASP239 4.2 29.6 1.0
O A:TYR235 4.2 24.8 1.0
CA A:GLY54 4.3 26.9 1.0
C A:VAL234 4.3 24.2 1.0
CE2 A:PHE220 4.4 29.4 1.0
C A:HIS53 4.5 25.1 1.0
CD1 A:TYR235 4.6 26.7 1.0
CB A:VAL236 4.6 24.7 1.0
N A:TYR235 4.6 24.4 1.0
C8 A:1V7601 4.6 28.1 1.0
CB A:ASP239 4.8 26.3 1.0
CA A:HIS53 4.9 24.8 1.0
CG A:ASP239 4.9 28.1 1.0
O A:HIS53 5.0 24.4 1.0

Reference:

J.Yi, Z.Cai, H.Qiu, F.Lu, Z.Luo, B.Chen, Q.Gu, J.Xu, H.Zhou. Fragment Screening and Structural Analyses Highlight the Atp-Assisted Ligand Binding For Inhibitor Discovery Against Type 1 Methionyl-Trna Synthetase. Nucleic Acids Res. V. 50 4755 2022.
ISSN: ESSN 1362-4962
PubMed: 35474479
DOI: 10.1093/NAR/GKAC285
Page generated: Thu Jul 11 04:41:29 2024

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