Fluorine in PDB 3kvz: Structural Basis of the Activity and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan

The structure of Structural Basis of the Activity and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan, PDB code: 3kvz 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)	33.70 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	79.500, 70.890, 102.880, 90.00, 103.06, 90.00
R / Rfree (%)	20.4 / 28.2

The binding sites of Fluorine atom in the Structural Basis of the Activity and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan (pdb code 3kvz). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Structural Basis of the Activity and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan, PDB code: 3kvz:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Structural Basis of the Activity and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan


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 and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:40.4 occ:1.00 F4 B:ENV201 0.0 40.4 1.0 C3 B:ENV201 1.4 41.3 1.0 OE2 A:GLU50 2.3 29.2 1.0 C2 B:ENV201 2.5 40.5 1.0 CD A:GLU50 3.0 29.8 1.0 N B:GLY43 3.1 14.4 1.0 O5 B:ENV201 3.2 42.4 1.0 C4 B:ENV201 3.5 39.6 1.0 CD2 B:LEU26 3.5 19.9 1.0 OE1 A:GLU50 3.5 31.9 1.0 N B:THR42 3.8 16.4 1.0 CB B:THR42 3.9 16.0 1.0 CA B:GLY43 3.9 14.4 1.0 CA A:GLY47 3.9 16.1 1.0 CG A:GLU50 4.0 24.4 1.0 C B:THR42 4.0 15.5 1.0 CA B:THR42 4.1 15.9 1.0 CG1 A:VAL46 4.1 20.4 1.0 N A:GLY47 4.2 17.9 1.0 CB B:ALA41 4.4 14.8 1.0 C B:ALA41 4.5 16.6 1.0 CB A:GLU50 4.5 21.0 1.0 OG1 B:THR42 4.6 17.0 1.0 C A:VAL46 4.7 17.8 1.0 O A:HOH512 4.8 38.2 1.0 C6 B:ENV201 4.8 39.7 1.0 O A:VAL46 4.8 19.9 1.0 CA B:ALA41 4.9 16.4 1.0 CG2 B:THR42 4.9 16.2 1.0 CG B:LEU26 4.9 22.9 1.0

Fluorine binding site 2 out of 2 in the Structural Basis of the Activity and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan


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 and Substrate Specificity of the Fluoroacetyl-Coa Thiesterase Flk - Wild Type Flk in Complex with Faccpan within 5.0Å range: probe atom residue distance (Å) B Occ E:F202 b:39.8 occ:1.00 F4 E:ENV202 0.0 39.8 1.0 C3 E:ENV202 1.4 42.2 1.0 C2 E:ENV202 2.5 42.2 1.0 OE2 E:GLU50 2.5 30.1 1.0 CD E:GLU50 3.0 24.8 1.0 N F:GLY43 3.0 14.5 1.0 O5 E:ENV202 3.1 39.2 1.0 C6 E:ENV202 3.4 45.1 1.0 CD2 F:LEU26 3.4 15.6 1.0 OE1 E:GLU50 3.5 29.5 1.0 C4 E:ENV202 3.5 42.8 1.0 CA F:GLY43 3.7 14.7 1.0 CA E:GLY47 3.7 17.6 1.0 CB F:THR42 3.8 14.0 1.0 CG E:GLU50 3.8 19.8 1.0 N F:THR42 3.9 14.7 1.0 C F:THR42 4.0 14.6 1.0 CG1 E:VAL46 4.0 20.5 1.0 N E:GLY47 4.1 17.1 1.0 CA F:THR42 4.1 14.2 1.0 O E:VAL46 4.3 19.3 1.0 C E:VAL46 4.4 18.6 1.0 CB E:GLU50 4.4 14.7 1.0 C7 E:ENV202 4.6 45.9 1.0 OG1 F:THR42 4.6 14.0 1.0 CG2 F:THR42 4.6 12.6 1.0 CB F:ALA41 4.7 12.7 1.0 C F:ALA41 4.7 14.2 1.0 O E:GLY43 4.8 18.8 1.0 CG F:LEU26 5.0 16.9 1.0 C E:GLY47 5.0 17.0 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