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Chlorine in PDB 3q19: Human Glutathione Transferase O2

Enzymatic activity of Human Glutathione Transferase O2

All present enzymatic activity of Human Glutathione Transferase O2:
2.5.1.18;

Protein crystallography data

The structure of Human Glutathione Transferase O2, PDB code: 3q19 was solved by H.Zhou, P.G.Board, A.J.Oakley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.51 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.425, 85.017, 60.397, 90.00, 94.55, 90.00
R / Rfree (%) 16.4 / 19.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Glutathione Transferase O2 (pdb code 3q19). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Glutathione Transferase O2, PDB code: 3q19:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3q19

Go back to Chlorine Binding Sites List in 3q19
Chlorine binding site 1 out of 2 in the Human Glutathione Transferase O2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Glutathione Transferase O2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl241

b:20.2
occ:0.66
OG A:SER205 2.9 23.3 1.0
O A:HOH243 2.9 13.9 1.0
O A:HOH252 3.1 16.8 1.0
CG2 A:ILE204 3.8 22.5 1.0
CA A:SER205 3.8 23.2 1.0
N A:SER205 3.8 22.7 1.0
CB A:SER205 3.9 24.0 1.0
CD A:LYS208 4.0 27.1 1.0
CE A:LYS208 4.2 26.3 1.0
C A:ILE204 4.2 22.4 1.0
NZ A:LYS208 4.4 28.2 1.0
CB A:ILE204 4.5 22.1 1.0
O A:ILE204 4.6 22.6 1.0
O A:ARG201 4.7 25.4 1.0
CG A:LYS208 5.0 22.8 1.0

Chlorine binding site 2 out of 2 in 3q19

Go back to Chlorine Binding Sites List in 3q19
Chlorine binding site 2 out of 2 in the Human Glutathione Transferase O2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Glutathione Transferase O2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl241

b:21.4
occ:0.66
OG B:SER205 2.9 23.2 1.0
O B:HOH343 3.0 17.6 1.0
CA B:SER205 3.7 22.1 1.0
CG2 B:ILE204 3.9 20.7 1.0
CB B:SER205 3.9 22.9 1.0
N B:SER205 3.9 21.2 1.0
CE B:LYS208 4.0 27.2 1.0
CD B:LYS208 4.2 27.4 1.0
C B:ILE204 4.3 20.4 1.0
NZ B:LYS208 4.4 27.9 1.0
CB B:ILE204 4.6 20.3 1.0
O B:HOH341 4.6 22.4 1.0
O B:ILE204 4.7 20.9 1.0
CG B:LYS208 4.7 25.4 1.0
O B:ARG201 4.7 21.8 1.0
O B:HOH253 4.9 29.5 1.0

Reference:

H.Zhou, J.Brock, D.Liu, P.G.Board, A.J.Oakley. Structural Insights Into the Dehydroascorbate Reductase Activity of Human Omega-Class Glutathione Transferases. J.Mol.Biol. V. 420 190 2012.
ISSN: ISSN 0022-2836
PubMed: 22522127
DOI: 10.1016/J.JMB.2012.04.014
Page generated: Fri Jul 11 09:16:38 2025

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