Bromine in PDB 1aqv: Glutathione S-Transferase in Complex with P-Bromobenzylglutathione

All present enzymatic activity of Glutathione S-Transferase in Complex with P-Bromobenzylglutathione:
2.5.1.18;

The structure of Glutathione S-Transferase in Complex with P-Bromobenzylglutathione, PDB code: 1aqv was solved by L.Prade, R.Huber, T.H.Manoharan, W.E.Fahl, W.Reuter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.94
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.660, 90.070, 69.570, 90.00, 99.19, 90.00
R / Rfree (%)	19.4 / 25.2

The binding sites of Bromine atom in the Glutathione S-Transferase in Complex with P-Bromobenzylglutathione (pdb code 1aqv). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Glutathione S-Transferase in Complex with P-Bromobenzylglutathione, PDB code: 1aqv:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Glutathione S-Transferase in Complex with P-Bromobenzylglutathione


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Glutathione S-Transferase in Complex with P-Bromobenzylglutathione within 5.0Å range: probe atom residue distance (Å) B Occ A:Br2201 b:43.9 occ:1.00 BR A:0HG2201 0.0 43.9 1.0 C4 A:0HG2201 1.9 35.0 1.0 C5 A:0HG2201 2.8 31.9 1.0 C3 A:0HG2201 2.9 34.6 1.0 CA A:GLY205 4.0 24.9 1.0 CG A:PHE8 4.0 23.9 1.0 CB A:PHE8 4.1 17.8 1.0 CG2 A:VAL35 4.1 45.9 1.0 C6 A:0HG2201 4.2 28.4 1.0 CD1 A:PHE8 4.2 23.6 1.0 C2 A:0HG2201 4.2 31.5 1.0 CD2 A:PHE8 4.5 22.6 1.0 O A:GLY205 4.6 27.8 1.0 CG1 A:VAL10 4.6 14.6 1.0 C11 A:0HG2201 4.7 30.2 1.0 C A:GLY205 4.8 25.9 1.0 CE1 A:PHE8 4.8 23.0 1.0 O A:HOH3133 4.9 57.0 1.0

Bromine binding site 2 out of 2 in the Glutathione S-Transferase in Complex with P-Bromobenzylglutathione


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Glutathione S-Transferase in Complex with P-Bromobenzylglutathione within 5.0Å range: probe atom residue distance (Å) B Occ B:Br2101 b:45.2 occ:1.00 BR B:0HG2101 0.0 45.2 1.0 C4 B:0HG2101 1.9 36.7 1.0 C5 B:0HG2101 2.8 33.9 1.0 C3 B:0HG2101 2.9 36.0 1.0 CG2 B:VAL35 3.9 39.3 1.0 CG B:PHE8 4.0 21.2 1.0 CA B:GLY205 4.0 22.4 1.0 CD1 B:PHE8 4.1 19.9 1.0 CB B:PHE8 4.1 17.3 1.0 C6 B:0HG2101 4.1 33.1 1.0 C2 B:0HG2101 4.2 33.1 1.0 O B:GLY205 4.4 26.2 1.0 CD2 B:PHE8 4.5 20.9 1.0 C B:GLY205 4.6 24.2 1.0 CE1 B:PHE8 4.7 21.2 1.0 C11 B:0HG2101 4.7 32.0 1.0 CG1 B:VAL10 4.7 13.7 1.0

L.Prade, R.Huber, T.H.Manoharan, W.E.Fahl, W.Reuter. Structures of Class Pi Glutathione S-Transferase From Human Placenta in Complex with Substrate, Transition-State Analogue and Inhibitor. Structure V. 5 1287 1997.
ISSN: ISSN 0969-2126
PubMed: 9351803
DOI: 10.1016/S0969-2126(97)00281-5