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Fluorine in PDB 5fwg: Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase

Enzymatic activity of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase

All present enzymatic activity of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase:
2.5.1.18;

Protein crystallography data

The structure of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase, PDB code: 5fwg was solved by J.F.Parsons, G.Xiao, R.N.Armstrong, G.L.Gilliland, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 86.939, 68.747, 80.539, 90.00, 105.08, 90.00
R / Rfree (%) n/a / n/a

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase (pdb code 5fwg). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 8 binding sites of Fluorine where determined in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase, PDB code: 5fwg:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Fluorine binding site 1 out of 8 in 5fwg

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Fluorine binding site 1 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F7

b:37.0
occ:1.00
 F A:FTR7 0.0 37.0 1.0
CZ3 A:FTR7 1.3 80.8 1.0
CE3 A:FTR7 2.3 19.2 1.0
CH2 A:FTR7 2.4 22.6 1.0
CA A:MET34 3.5 38.5 1.0
CB A:MET34 3.5 38.3 1.0
N A:MET34 3.6 39.1 1.0
CD2 A:FTR7 3.6 48.9 1.0
CZ2 A:FTR7 3.6 0.0 1.0
C A:ALA33 3.7 39.0 1.0
O A:ALA33 3.7 44.5 1.0
CG A:ARG42 3.8 42.0 1.0
CA A:ARG42 3.9 30.3 1.0
CE2 A:FTR7 4.1 30.6 1.0
O A:ARG42 4.1 24.9 1.0
CB A:TYR32 4.2 20.3 1.0
CB A:ARG42 4.2 32.1 1.0
C A:ARG42 4.3 23.8 1.0
CB A:FTR45 4.3 19.9 1.0
N A:ALA33 4.3 32.8 1.0
O A:ASP41 4.4 48.9 1.0
C A:TYR32 4.5 29.7 1.0
CA A:ALA33 4.5 29.6 1.0
CE A:MET34 4.6 38.6 1.0
N A:FTR45 4.6 20.4 1.0
O A:TYR32 4.7 41.8 1.0
CG A:MET34 4.7 44.2 1.0
C A:MET34 4.9 34.6 1.0
CG A:FTR7 4.9 48.5 1.0
O A:HOH826 4.9 22.8 0.9
CA A:TYR32 5.0 17.6 1.0

Fluorine binding site 2 out of 8 in 5fwg

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Fluorine binding site 2 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F45

b:37.0
occ:1.00
 F A:FTR45 0.0 37.0 1.0
CZ3 A:FTR45 1.3 30.8 1.0
CE3 A:FTR45 2.3 18.3 1.0
CH2 A:FTR45 2.3 19.6 1.0
CE2 A:TYR61 3.0 20.4 1.0
CD1 A:LEU52 3.0 46.1 1.0
CD2 A:TYR61 3.5 21.5 1.0
CD2 A:FTR45 3.6 20.9 1.0
CZ2 A:FTR45 3.6 27.9 1.0
OH A:TYR32 3.7 36.0 1.0
CZ A:TYR61 4.0 7.8 1.0
CZ A:TYR32 4.0 33.3 1.0
CE2 A:FTR45 4.0 12.7 1.0
CD2 A:LEU59 4.1 27.6 1.0
CE2 A:TYR32 4.1 32.2 1.0
CA A:LYS49 4.2 19.2 1.0
N A:LYS49 4.3 20.6 1.0
O A:GLU48 4.3 17.0 1.0
OH A:TYR61 4.3 39.8 1.0
CG A:LEU52 4.4 38.5 1.0
C A:GLU48 4.4 17.3 1.0
O A:FTR45 4.6 26.7 1.0
CD1 A:LEU54 4.6 25.8 1.0
CG A:TYR61 4.7 19.8 1.0
O A:LYS49 4.7 17.4 1.0
CB A:GLU48 4.8 19.6 1.0
O A:ASN58 4.8 16.6 1.0
CG A:FTR45 4.9 23.5 1.0
C A:LYS49 4.9 29.1 1.0
CE1 A:TYR32 4.9 25.4 1.0
CG A:LYS49 5.0 34.9 1.0
CB A:LYS49 5.0 16.1 1.0

Fluorine binding site 3 out of 8 in 5fwg

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Fluorine binding site 3 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F146

b:51.4
occ:1.00
 F A:FTR146 0.0 51.4 1.0
CZ3 A:FTR146 1.4 74.5 1.0
CH2 A:FTR146 2.4 24.1 1.0
CE3 A:FTR146 2.4 20.7 1.0
CE1 A:PHE183 3.2 27.9 1.0
CA A:PHE187 3.4 25.3 1.0
CB A:PHE187 3.5 17.7 1.0
CZ2 A:FTR146 3.6 24.7 1.0
CD1 A:PHE187 3.6 28.3 1.0
CD2 A:FTR146 3.6 36.9 1.0
N A:PHE187 3.7 19.5 1.0
CD1 A:PHE183 3.7 19.6 1.0
CZ A:PHE183 4.0 15.6 1.0
CG A:PHE187 4.0 25.2 1.0
CE2 A:FTR146 4.1 37.7 1.0
CD1 A:LEU190 4.1 41.9 1.0
O A:PHE183 4.2 24.1 1.0
CB A:ASP156 4.3 19.4 1.0
C A:ARG186 4.4 31.9 1.0
CG A:ASP156 4.5 18.0 1.0
OD2 A:ASP156 4.7 27.9 1.0
CB A:ARG186 4.7 35.1 1.0
NE A:ARG186 4.8 27.7 1.0
CE1 A:PHE187 4.8 26.1 1.0
O A:ARG186 4.8 30.4 1.0
C A:PHE187 4.8 32.3 1.0
CG A:PHE183 4.9 17.8 1.0
CG A:FTR146 5.0 21.0 1.0

Fluorine binding site 4 out of 8 in 5fwg

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Fluorine binding site 4 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F214

b:39.7
occ:1.00
 F A:FTR214 0.0 39.7 1.0
CZ3 A:FTR214 1.3 23.3 1.0
CE3 A:FTR214 2.4 0.0 1.0
CH2 A:FTR214 2.4 45.1 1.0
CD1 A:ILE207 3.0 69.0 1.0
CE2 A:PHE208 3.0 68.7 1.0
CG1 A:ILE207 3.2 40.9 1.0
CD2 A:LEU110 3.4 26.9 1.0
CD2 A:FTR214 3.6 38.1 1.0
CZ2 A:FTR214 3.6 26.1 1.0
CZ A:PHE208 3.7 62.2 1.0
CD2 A:PHE208 3.7 67.0 1.0
CE2 A:FTR214 4.1 30.7 1.0
CG A:LEU110 4.1 34.8 1.0
CB A:SER215 4.4 32.5 1.0
CB A:ILE207 4.5 38.6 1.0
SG A:CYS114 4.6 36.1 1.0
CD1 A:LEU110 4.7 32.1 1.0
NE2 A:GLN165 4.7 24.8 1.0
CD1 A:PHE169 4.8 23.9 1.0
CE1 A:PHE208 4.8 58.4 1.0
O A:GLN165 4.9 34.9 1.0
CG A:PHE208 4.9 55.8 1.0
CB A:GLN165 4.9 19.3 1.0
CG A:FTR214 4.9 24.3 1.0
OG A:SER215 5.0 37.1 1.0

Fluorine binding site 5 out of 8 in 5fwg

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Fluorine binding site 5 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F7

b:23.0
occ:1.00
 F B:FTR7 0.0 23.0 1.0
CZ3 B:FTR7 1.3 23.4 1.0
CE3 B:FTR7 2.3 20.8 1.0
CH2 B:FTR7 2.4 45.4 1.0
C B:ALA33 3.4 22.4 1.0
CB B:TYR32 3.5 34.2 1.0
N B:MET34 3.5 30.1 1.0
CZ2 B:FTR7 3.6 71.4 1.0
CD2 B:FTR7 3.6 40.9 1.0
O B:ALA33 3.7 31.4 1.0
N B:ALA33 3.7 22.8 1.0
C B:TYR32 3.9 40.2 1.0
CG B:MET34 3.9 47.1 1.0
CA B:MET34 3.9 31.9 1.0
CA B:ALA33 3.9 22.0 1.0
O B:TYR32 4.0 30.1 1.0
CE2 B:FTR7 4.1 25.5 1.0
O B:HOH565 4.1 22.5 0.8
CA B:ARG42 4.1 41.8 1.0
O B:ARG42 4.2 26.1 1.0
CB B:FTR45 4.2 40.7 1.0
CB B:MET34 4.4 34.3 1.0
OD1 B:ASN8 4.4 86.7 1.0
O B:ASP41 4.4 28.5 1.0
CA B:TYR32 4.4 35.1 1.0
C B:ARG42 4.5 26.8 1.0
N B:FTR45 4.6 23.8 1.0
CB B:ARG42 4.6 46.8 1.0
CG B:TYR32 4.6 28.1 1.0
CG B:ARG42 4.7 43.9 1.0
CB B:GLN44 4.8 41.3 1.0
CG B:FTR7 5.0 79.5 1.0

Fluorine binding site 6 out of 8 in 5fwg

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Fluorine binding site 6 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F45

b:38.0
occ:1.00
 F B:FTR45 0.0 38.0 1.0
CZ3 B:FTR45 1.3 14.8 1.0
CE3 B:FTR45 2.3 20.1 1.0
CH2 B:FTR45 2.3 18.5 1.0
CE2 B:TYR61 3.0 17.4 1.0
CD1 B:LEU52 3.0 31.0 1.0
OH B:TYR32 3.5 22.8 1.0
CD2 B:TYR61 3.5 11.1 1.0
CZ2 B:FTR45 3.6 34.3 1.0
CD2 B:FTR45 3.6 22.1 1.0
CZ B:TYR61 4.0 38.7 1.0
CE2 B:FTR45 4.0 20.9 1.0
CZ B:TYR32 4.1 30.9 1.0
CA B:LYS49 4.2 21.8 1.0
CD1 B:LEU54 4.2 13.2 1.0
CG B:LEU52 4.3 33.5 1.0
CD2 B:LEU59 4.3 14.7 1.0
CG B:GLU48 4.3 29.4 1.0
OH B:TYR61 4.3 26.3 1.0
O B:GLU48 4.4 15.9 1.0
N B:LYS49 4.5 20.2 1.0
C B:GLU48 4.5 15.4 1.0
OE2 B:GLU48 4.6 30.4 1.0
CE1 B:TYR32 4.6 12.9 1.0
O B:FTR45 4.7 20.9 1.0
O B:LYS49 4.7 18.7 1.0
CG B:TYR61 4.8 12.7 1.0
CE2 B:TYR32 4.9 17.0 1.0
C B:LYS49 4.9 20.5 1.0
CB B:LEU52 4.9 27.3 1.0
CG B:FTR45 4.9 14.6 1.0

Fluorine binding site 7 out of 8 in 5fwg

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Fluorine binding site 7 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F146

b:33.7
occ:1.00
 F B:FTR146 0.0 33.7 1.0
CZ3 B:FTR146 1.3 31.9 1.0
CE3 B:FTR146 2.3 30.2 1.0
CH2 B:FTR146 2.4 15.7 1.0
CE1 B:PHE183 3.1 17.7 1.0
CD1 B:PHE187 3.1 30.9 1.0
CB B:PHE187 3.3 22.1 1.0
CA B:PHE187 3.4 17.5 1.0
CZ B:PHE183 3.5 14.1 1.0
CD2 B:FTR146 3.6 16.0 1.0
CZ2 B:FTR146 3.6 16.2 1.0
CG B:PHE187 3.6 35.1 1.0
CD1 B:PHE183 3.8 23.2 1.0
CD2 B:LEU190 3.8 39.4 1.0
N B:PHE187 3.9 18.8 1.0
CB B:ASP156 4.1 26.2 1.0
CE2 B:FTR146 4.1 17.0 1.0
CE1 B:PHE187 4.2 23.0 1.0
O B:PHE183 4.4 24.0 1.0
CG B:ASP156 4.4 26.8 1.0
CE2 B:PHE183 4.5 18.8 1.0
C B:ARG186 4.5 35.7 1.0
OD1 B:ASP156 4.6 25.6 1.0
CG B:PHE183 4.7 18.3 1.0
C B:PHE187 4.7 34.8 1.0
O B:ARG186 4.7 40.6 1.0
CG B:FTR146 4.9 18.2 1.0
CD2 B:PHE183 4.9 21.4 1.0

Fluorine binding site 8 out of 8 in 5fwg

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Fluorine binding site 8 out of 8 in the Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Tetra-(5-Fluorotryptophanyl)-Glutathione Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F214

b:61.0
occ:1.00
 F B:FTR214 0.0 61.0 1.0
CZ3 B:FTR214 1.3 22.3 1.0
CH2 B:FTR214 2.3 45.6 1.0
CE3 B:FTR214 2.4 15.4 1.0
CE2 B:PHE208 3.2 36.8 1.0
CD1 B:ILE207 3.3 52.5 1.0
CZ2 B:FTR214 3.6 43.2 1.0
CD2 B:LEU110 3.6 31.3 1.0
CD2 B:FTR214 3.7 22.8 1.0
CB B:SER215 3.7 61.3 1.0
CZ B:PHE208 3.9 38.9 1.0
OG B:SER215 4.0 59.1 1.0
CD1 B:LEU110 4.0 43.9 1.0
CE2 B:FTR214 4.1 53.6 1.0
CG B:LEU110 4.1 43.8 1.0
CD2 B:PHE208 4.1 44.5 1.0
CD1 B:PHE169 4.3 48.2 1.0
CB B:GLN165 4.4 34.7 1.0
CB B:ILE207 4.4 37.2 1.0
CG1 B:ILE207 4.4 40.2 1.0
CG2 B:ILE207 4.5 26.1 1.0
SG B:CYS114 4.6 37.3 1.0
O B:GLN165 4.6 36.5 1.0
OE1 B:GLN165 4.7 49.1 1.0
CB B:PHE169 5.0 21.3 1.0
CE1 B:PHE169 5.0 42.7 1.0

Reference:

J.F.Parsons, G.Xiao, G.L.Gilliland, R.N.Armstrong. Enzymes Harboring Unnatural Amino Acids: Mechanistic and Structural Analysis of the Enhanced Catalytic Activity of A Glutathione Transferase Containing 5-Fluorotryptophan. Biochemistry V. 37 6286 1998.
ISSN: ISSN 0006-2960
PubMed: 9572843
DOI: 10.1021/BI980219E
Page generated: Thu Aug 1 09:29:17 2024

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