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Chlorine in PDB 1oyj: Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.

Enzymatic activity of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.

All present enzymatic activity of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione., PDB code: 1oyj was solved by D.P.Dixon, A.G.Mcewen, A.J.Lapthorn, R.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.829, 91.129, 165.034, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 22.7

Other elements in 1oyj:

The structure of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Chlorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Chlorine atom in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. (pdb code 1oyj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 20 binding sites of Chlorine where determined in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione., PDB code: 1oyj:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 20 in 1oyj

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Chlorine binding site 1 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl819

b:55.8
occ:1.00
 OD1 D:ASP205 4.5 30.3 1.0
O D:HOH904 4.6 47.7 1.0
O D:HOH868 4.6 50.5 1.0

Chlorine binding site 2 out of 20 in 1oyj

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Chlorine binding site 2 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl820

b:65.8
occ:1.00
 NZ B:LYS42 3.4 25.1 1.0
NE B:ARG54 3.4 34.2 1.0
CE B:LYS42 3.9 30.5 1.0
CD B:ARG54 4.0 31.2 1.0
CD B:LYS42 4.1 30.6 1.0
CB B:ARG54 4.3 25.0 1.0
CZ B:ARG54 4.4 44.6 1.0
NH2 B:ARG54 4.4 46.5 1.0
O B:HOH907 4.6 48.2 1.0
CG B:ARG54 4.7 26.4 1.0
CD2 B:LEU47 5.0 27.4 1.0

Chlorine binding site 3 out of 20 in 1oyj

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Chlorine binding site 3 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl821

b:51.5
occ:1.00
 NZ D:LYS216 3.0 25.8 0.3
CE D:LYS216 3.4 33.3 0.3
N D:SER213 3.4 30.7 1.0
CD D:LYS216 3.6 46.4 0.7
NZ D:LYS216 3.6 43.7 0.7
CE D:LYS216 3.6 45.8 0.7
CA D:PRO212 3.7 29.0 1.0
CD D:LYS216 3.9 36.0 0.3
C D:PRO212 4.0 30.2 1.0
OG D:SER213 4.2 31.7 1.0
CB D:SER213 4.2 32.6 1.0
CB D:PRO212 4.3 29.9 1.0
O D:HOH940 4.3 52.8 1.0
O D:HOH968 4.4 73.5 1.0
CA D:SER213 4.4 31.4 1.0
CG D:LYS216 4.5 38.7 0.3
CG D:LYS216 4.7 43.1 0.7
O D:HOH915 4.7 40.8 1.0
O D:LEU211 4.8 27.7 1.0
CB D:LYS216 4.9 39.9 1.0
N D:PRO212 5.0 28.6 1.0

Chlorine binding site 4 out of 20 in 1oyj

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Chlorine binding site 4 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl822

b:52.7
occ:1.00
 N C:GLY82 3.2 29.1 1.0
CB C:GLU3 3.4 62.0 1.0
C C:PHE80 3.5 25.0 1.0
CA C:PHE80 3.6 23.5 1.0
N C:GLU3 3.7 61.0 1.0
CA C:GLY82 3.7 29.8 1.0
N C:PRO81 3.7 26.6 1.0
CD C:PRO81 3.9 25.6 1.0
O C:PHE80 4.0 24.8 1.0
CB C:PHE80 4.0 24.5 1.0
CA C:GLU3 4.2 61.6 1.0
N C:THR83 4.2 29.1 1.0
C C:PRO81 4.2 28.4 1.0
C C:GLY82 4.2 30.1 1.0
CG2 C:THR83 4.3 28.9 1.0
CD2 C:PHE80 4.4 29.2 1.0
CA C:PRO81 4.5 27.7 1.0
CG C:GLU3 4.6 64.0 1.0
CG C:PRO81 4.7 28.4 1.0
CG C:PHE80 4.7 24.5 1.0
CD C:GLU3 4.8 68.4 1.0
OE1 C:GLU3 4.8 70.1 1.0
N C:PHE80 4.9 23.6 1.0
O C:ALA79 5.0 21.8 1.0

Chlorine binding site 5 out of 20 in 1oyj

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Chlorine binding site 5 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl823

b:58.6
occ:1.00
 N A:GLY82 3.1 29.7 1.0
C A:PHE80 3.5 26.7 1.0
CA A:PHE80 3.5 26.6 1.0
CA A:GLY82 3.6 30.8 1.0
O A:HOH938 3.6 54.9 1.0
N A:PRO81 3.7 28.4 1.0
CB A:PHE80 3.9 26.1 1.0
O A:PHE80 3.9 24.3 1.0
CD A:PRO81 4.0 29.7 1.0
N A:THR83 4.2 29.0 1.0
C A:GLY82 4.2 30.4 1.0
C A:PRO81 4.3 30.0 1.0
CG A:GLU4 4.3 69.4 1.0
CG2 A:THR83 4.4 27.0 1.0
CG A:PRO81 4.4 30.2 1.0
CD2 A:PHE80 4.4 28.7 1.0
OE2 A:GLU4 4.6 74.7 1.0
CA A:PRO81 4.6 28.6 1.0
CG A:PHE80 4.7 25.4 1.0
CD A:GLU4 4.9 72.7 1.0
N A:PHE80 4.9 26.6 1.0
O A:ALA79 5.0 28.9 1.0

Chlorine binding site 6 out of 20 in 1oyj

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Chlorine binding site 6 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl824

b:54.8
occ:1.00
 N3 C:GSH803 3.1 37.5 1.0
NZ C:LYS114 3.2 23.5 1.0
CD1 C:GSH803 3.4 45.7 1.0
O C:HOH920 3.5 49.8 1.0
N2 C:GSH803 3.6 36.1 1.0
CA3 C:GSH803 3.6 33.8 1.0
OE1 C:GSH803 3.7 39.1 1.0
CG1 C:GSH803 3.8 49.1 1.0
O31 C:GSH803 4.1 33.7 1.0
CB1 C:GSH803 4.1 58.5 1.0
C3 C:GSH803 4.2 35.5 1.0
C2 C:GSH803 4.2 37.7 1.0
O C:HOH1011 4.3 52.9 1.0
CA2 C:GSH803 4.3 36.7 1.0
O C:HOH967 4.5 47.4 1.0
O C:HOH901 4.6 49.5 1.0
O C:HOH1039 4.6 51.0 1.0
CE C:LYS114 4.6 26.5 1.0
O C:HOH1021 4.9 49.3 1.0

Chlorine binding site 7 out of 20 in 1oyj

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Chlorine binding site 7 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl825

b:66.0
occ:1.00
 N A:LEU45 3.2 26.1 1.0
N A:ASP44 3.6 23.6 1.0
CB A:LEU45 3.7 26.3 1.0
CB A:SER43 3.7 22.7 1.0
CB A:ASP44 3.8 25.9 1.0
CA A:ASP44 4.0 25.7 1.0
OG A:SER43 4.0 22.3 1.0
C A:ASP44 4.0 25.4 1.0
CA A:LEU45 4.0 25.8 1.0
C A:SER43 4.2 22.6 1.0
CA A:SER43 4.5 22.6 1.0
O A:HOH883 4.7 53.6 1.0
CG A:ASP44 4.9 30.0 1.0

Chlorine binding site 8 out of 20 in 1oyj

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Chlorine binding site 8 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl826

b:73.3
occ:1.00
 N A:LYS126 3.0 24.1 1.0
CG A:LYS126 3.3 29.1 1.0
O A:LYS126 3.5 19.9 1.0
CA A:LEU125 3.7 27.6 1.0
C A:LEU125 3.8 26.1 1.0
CA A:LYS126 3.9 23.2 1.0
CB A:LEU125 3.9 27.9 1.0
O A:HOH889 3.9 74.0 1.0
CG A:PRO129 4.0 20.6 1.0
CB A:PRO129 4.0 19.3 1.0
C A:LYS126 4.1 22.8 1.0
CD2 A:LEU125 4.1 33.2 1.0
CB A:LYS126 4.2 25.4 1.0
CD A:LYS126 4.3 35.7 1.0
CE A:LYS126 4.4 39.2 1.0
CD A:PRO129 4.6 19.1 1.0
CG A:LEU125 4.6 28.8 1.0
O A:ARG124 4.9 31.8 1.0
O A:LEU125 4.9 25.5 1.0

Chlorine binding site 9 out of 20 in 1oyj

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Chlorine binding site 9 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl827

b:62.7
occ:1.00
 N A:PHE153 3.1 20.3 1.0
N A:GLU152 3.4 19.1 1.0
CB A:GLU152 3.6 21.3 1.0
O A:PHE153 3.7 20.8 1.0
O A:GLY155 3.8 43.6 1.0
CA A:GLU152 3.9 20.0 1.0
N A:GLY158 3.9 53.6 1.0
CA A:PHE153 4.0 21.7 1.0
C A:GLU152 4.0 20.0 1.0
CB A:ARG151 4.0 23.1 1.0
CB A:PHE153 4.0 22.3 1.0
C A:PHE153 4.3 22.3 1.0
CD2 A:PHE153 4.3 24.6 1.0
C A:ARG151 4.3 20.3 1.0
CA A:ARG151 4.5 20.6 1.0
CA A:GLY157 4.6 53.6 1.0
CA A:GLY158 4.7 52.9 1.0
CG A:PHE153 4.7 24.8 1.0
C A:GLY157 4.8 53.7 1.0
OE1 A:GLU152 4.8 34.9 1.0
CG A:GLU152 4.9 26.9 1.0
CG A:ARG151 4.9 26.9 1.0

Chlorine binding site 10 out of 20 in 1oyj

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Chlorine binding site 10 out of 20 in the Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Crystal Structure Solution of Rice GST1 (OSGSTU1) in Complex with Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl828

b:67.0
occ:1.00
 N C:ASP205 3.1 20.9 1.0
CG C:ASP205 3.5 26.8 1.0
OD2 C:ASP205 3.6 29.7 1.0
CB C:ASP205 3.7 23.3 1.0
CA C:ILE204 3.8 24.5 1.0
OD1 C:ASP205 3.8 32.6 1.0
O C:HOH947 3.8 44.3 1.0
C C:ILE204 3.9 23.0 1.0
CA C:ASP205 4.0 23.4 1.0
CG2 C:ILE204 4.0 23.7 1.0
O C:ARG203 4.3 27.0 1.0
CB C:ILE204 4.4 24.1 1.0
O C:HOH896 4.5 43.1 1.0
O B:HOH894 4.6 63.2 1.0
O B:GLY184 4.8 39.2 1.0
N C:ILE204 4.9 24.7 1.0
CG1 C:ILE204 5.0 26.1 1.0

Reference:

D.P.Dixon, A.G.Mcewen, A.J.Lapthorn, R.Edwards. Forced Evolution of A Herbicide Detoxifying Glutathione Transferase. J.Biol.Chem. V. 278 23930 2003.
ISSN: ISSN 0021-9258
PubMed: 12692133
DOI: 10.1074/JBC.M303620200
Page generated: Thu Jul 10 18:46:44 2025

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