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

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

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

Protein crystallography data

The structure of Methionyl-Trna Synthetase From Staphylococcus Aureus Complexed with A Phenylbenzimidazole Inhibitor and Atp, PDB code: 7wpn 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) 61.13 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.487, 72.053, 115.488, 90, 90, 90
R / Rfree (%) 21.7 / 25.9

Bromine Binding Sites:

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

Bromine binding site 1 out of 1 in 7wpn

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


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 and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br603

b:15.9
occ:1.00
 BR A:29I603 0.0 15.9 1.0
C12 A:29I603 1.9 17.4 1.0
C11 A:29I603 2.8 17.8 1.0
C13 A:29I603 2.8 17.6 1.0
O1 A:29I603 3.1 17.7 1.0
O A:VAL234 3.2 16.7 1.0
N A:VAL236 3.4 16.9 1.0
O A:HOH703 3.6 9.2 1.0
C A:TYR235 3.6 16.7 1.0
CZ A:PHE220 3.8 19.5 1.0
CA A:TYR235 3.8 16.8 1.0
OD2 A:ASP239 3.9 14.9 1.0
CA A:VAL236 3.9 17.2 1.0
CB A:HIS53 4.0 16.0 1.0
N A:GLY54 4.1 16.9 1.0
C10 A:29I603 4.1 18.2 1.0
C14 A:29I603 4.1 18.1 1.0
O A:TYR235 4.1 16.6 1.0
CE2 A:PHE220 4.2 19.3 1.0
C A:VAL234 4.2 16.9 1.0
CA A:GLY54 4.4 17.4 1.0
C A:HIS53 4.4 16.5 1.0
N A:TYR235 4.5 16.7 1.0
CB A:VAL236 4.5 17.3 1.0
CD1 A:TYR235 4.6 16.9 1.0
CB A:ASP239 4.6 15.1 1.0
C9 A:29I603 4.7 18.7 1.0
CG A:ASP239 4.8 15.1 1.0
CA A:HIS53 4.8 16.1 1.0
CE1 A:PHE220 4.9 19.6 1.0
O A:HIS53 4.9 16.4 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: Mon Jul 7 11:54:39 2025

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