Fluorine in PDB 3kuw: Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate

The structure of Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate, PDB code: 3kuw was solved by M.V.B.Dias, F.Huang, D.Y.Chirgadze, M.Tosin, D.Spiteller, E.F.Valentine, P.F.Leadlay, J.B.Spencer, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.45 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	62.504, 92.896, 49.594, 90.00, 100.93, 90.00
R / Rfree (%)	18.5 / 25.6

The binding sites of Fluorine atom in the Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate (pdb code 3kuw). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate, PDB code: 3kuw:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:F140 b:44.9 occ:1.00 F A:FAH140 0.0 44.9 1.0 CH3 A:FAH140 1.4 44.2 1.0 C A:FAH140 2.6 44.4 1.0 O A:HOH426 2.6 25.4 1.0 O B:HOH365 2.9 36.5 1.0 OXT A:FAH140 3.0 43.5 1.0 OE1 A:GLU50 3.1 23.3 1.0 NH2 A:ARG120 3.4 10.7 1.0 NH1 A:ARG120 3.6 7.4 1.0 CE1 B:PHE36 3.6 23.8 1.0 O A:FAH140 3.7 44.2 1.0 N A:GLY69 3.9 14.9 1.0 CZ A:ARG120 4.0 15.9 1.0 CD1 B:PHE36 4.3 23.0 1.0 CD A:GLU50 4.4 21.4 1.0 CZ B:PHE36 4.5 22.9 1.0 CA A:GLY69 4.6 13.9 1.0 C A:LEU68 4.8 15.9 1.0 CA A:LEU68 4.8 17.3 1.0 O A:SER67 4.8 14.9 1.0 O B:HOH162 4.9 12.7 1.0 CB A:GLU50 4.9 11.9 1.0 CG2 B:VAL23 4.9 13.8 1.0 CG1 B:VAL23 5.0 13.1 1.0

Fluorine binding site 2 out of 4 in the Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:F141 b:44.5 occ:1.00 F A:FAH141 0.0 44.5 1.0 CH3 A:FAH141 1.4 41.2 1.0 C A:FAH141 2.3 40.9 1.0 OXT A:FAH141 2.8 39.9 1.0 CD2 B:LEU68 2.9 25.5 1.0 O A:FAH141 3.3 38.7 1.0 F A:FAH142 3.4 41.0 1.0 CE2 A:PHE36 3.7 27.8 1.0 O B:HOH433 3.9 30.8 1.0 CZ A:PHE36 3.9 30.9 1.0 O A:FAH142 4.0 43.5 1.0 CG2 A:VAL23 4.1 16.2 1.0 CG B:LEU68 4.1 18.8 1.0 CA B:LEU68 4.2 13.6 1.0 CG2 A:VAL39 4.2 13.5 1.0 CB B:LEU68 4.3 14.5 1.0 N B:GLY69 4.4 11.6 1.0 CH3 A:FAH142 4.4 44.1 1.0 C A:FAH142 4.6 43.7 1.0 CD2 A:PHE36 4.7 27.5 1.0 O B:HOH434 4.8 28.2 1.0 C B:LEU68 4.9 12.4 1.0 O B:SER67 4.9 13.8 1.0 CD1 B:LEU68 5.0 19.1 1.0

Fluorine binding site 3 out of 4 in the Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:F142 b:41.0 occ:1.00 F A:FAH142 0.0 41.0 1.0 CH3 A:FAH142 1.4 44.1 1.0 C A:FAH142 2.5 43.7 1.0 O A:HOH184 2.9 12.9 1.0 O A:FAH142 3.0 43.5 1.0 CH3 A:FAH141 3.2 41.2 1.0 F A:FAH141 3.4 44.5 1.0 OXT A:FAH142 3.5 44.3 1.0 CB A:ALA79 3.7 14.4 1.0 CG2 A:VAL39 3.8 13.5 1.0 CA A:ALA79 3.9 15.0 1.0 CD2 B:LEU68 4.0 25.5 1.0 CE1 A:HIS76 4.0 17.5 1.0 NE2 A:HIS76 4.1 20.6 1.0 O A:PHE40 4.3 12.8 1.0 CB A:VAL39 4.4 13.7 1.0 C A:FAH141 4.5 40.9 1.0 O A:ALA78 4.5 14.3 1.0 ND1 A:HIS76 4.6 17.5 1.0 N A:ALA79 4.7 15.5 1.0 CD2 A:HIS76 4.7 19.8 1.0 CD1 B:LEU68 4.7 19.1 1.0 OXT A:FAH141 4.7 39.9 1.0 CZ B:PHE128 4.8 13.4 1.0 C A:ALA78 4.9 14.8 1.0 O A:HOH160 4.9 19.5 1.0 CG B:LEU68 4.9 18.8 1.0 CG A:HIS76 5.0 14.7 1.0

Fluorine binding site 4 out of 4 in the Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structural Basis of the Activity Ans Substrate Specificity of the Fluoroacetyl-Coa Thioesterase Flk - T42S Mutant in Complex with Fluoro-Acetate within 5.0Å range: probe atom residue distance (Å) B Occ B:F140 b:54.5 occ:1.00 F B:FAH140 0.0 54.5 1.0 CH3 B:FAH140 1.4 55.6 1.0 C B:FAH140 2.3 56.0 1.0 OXT B:FAH140 3.0 56.3 1.0 O B:FAH140 3.1 56.7 1.0 OG A:SER42 3.2 17.6 1.0 CD B:GLU50 3.3 22.9 1.0 CB A:SER42 3.4 13.1 1.0 OE2 B:GLU50 3.4 28.1 1.0 NE2 B:HIS118 3.4 13.1 1.0 OE1 B:GLU50 3.5 20.6 1.0 O B:HOH367 3.7 39.9 1.0 CA B:GLY69 3.7 10.8 1.0 CG B:GLU50 3.8 15.0 1.0 CD2 B:HIS118 4.0 8.3 1.0 C B:GLY69 4.0 12.1 1.0 OXT A:FAH141 4.2 39.9 1.0 O B:GLY69 4.2 11.8 1.0 CG1 B:VAL46 4.4 10.9 1.0 CE1 B:HIS118 4.5 6.8 1.0 O B:ALA71 4.6 12.0 1.0 N B:THR70 4.7 11.5 1.0 CB B:ILE72 4.7 12.5 1.0 N B:GLY69 4.8 11.6 1.0 C B:ALA71 4.8 9.4 1.0 N B:ALA71 4.9 8.8 1.0 CA A:SER42 4.9 12.5 1.0 CG2 B:ILE72 5.0 14.0 1.0

M.V.Dias, F.Huang, D.Y.Chirgadze, M.Tosin, D.Spiteller, E.F.Dry, P.F.Leadlay, J.B.Spencer, T.L.Blundell. Structural Basis For the Activity and Substrate Specificity of Fluoroacetyl-Coa Thioesterase Flk. J.Biol.Chem. V. 285 22495 2010.
ISSN: ISSN 0021-9258
PubMed: 20430898
DOI: 10.1074/JBC.M110.107177