Fluorine in PDB 7fwf: Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid

The structure of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid, PDB code: 7fwf was solved by A.Ehler, J.Benz, U.Obst, H.Richter, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.08 / 1.24
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.03, 52.808, 72.159, 90, 90, 90
R / Rfree (%)	13.6 / 18

The binding sites of Fluorine atom in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid (pdb code 7fwf). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid, PDB code: 7fwf:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F203 b:22.9 occ:1.00 F09 A:MQF203 0.0 22.9 1.0 C08 A:MQF203 1.3 18.0 1.0 F10 A:MQF203 2.2 20.6 1.0 F11 A:MQF203 2.2 21.7 1.0 C04 A:MQF203 2.3 15.6 1.0 HG21 A:ILE104 2.8 11.2 1.0 O19 A:MQF203 3.1 16.4 1.0 N03 A:MQF203 3.1 14.4 1.0 C05 A:MQF203 3.1 13.6 1.0 HG12 A:ILE104 3.3 12.2 1.0 C17 A:MQF203 3.4 15.9 1.0 HH21 A:ARG106 3.4 20.9 1.0 HH22 A:ARG106 3.5 20.4 1.0 O A:HOH353 3.6 18.7 1.0 NH2 A:ARG106 3.6 22.3 1.0 CG2 A:ILE104 3.7 11.5 1.0 HG11 A:VAL115 3.9 12.5 1.0 HG23 A:ILE104 4.0 11.3 1.0 HG A:CYS117 4.2 16.6 1.0 CG1 A:ILE104 4.2 12.2 1.0 HG22 A:ILE104 4.3 11.3 1.0 C02 A:MQF203 4.3 11.9 1.0 C06 A:MQF203 4.3 12.9 1.0 O A:HOH398 4.4 26.6 1.0 O18 A:MQF203 4.5 14.7 1.0 HG12 A:VAL115 4.5 12.2 1.0 SG A:CYS117 4.5 17.6 1.0 CZ A:ARG106 4.5 16.6 1.0 CB A:ILE104 4.6 10.3 1.0 H28 A:MQF203 4.6 14.4 1.0 CG1 A:VAL115 4.6 12.6 1.0 O A:HOH339 4.6 18.0 1.0 HG13 A:ILE104 4.8 12.5 1.0 HD13 A:ILE104 4.8 15.1 1.0 C01 A:MQF203 4.9 12.6 1.0 HG13 A:VAL115 4.9 11.8 1.0 HB A:ILE104 4.9 10.4 1.0 HE A:ARG106 5.0 14.8 1.0 CD1 A:ILE104 5.0 16.1 1.0

Fluorine binding site 2 out of 6 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F203 b:20.6 occ:1.00 F10 A:MQF203 0.0 20.6 1.0 C08 A:MQF203 1.3 18.0 1.0 F11 A:MQF203 2.2 21.7 1.0 F09 A:MQF203 2.2 22.9 1.0 C04 A:MQF203 2.3 15.6 1.0 N03 A:MQF203 2.6 14.4 1.0 HG A:CYS117 2.7 16.6 1.0 HG12 A:ILE104 3.2 12.2 1.0 SG A:CYS117 3.3 17.6 1.0 HE2 A:TYR19 3.4 8.9 1.0 HE1 A:PHE16 3.5 10.1 1.0 C05 A:MQF203 3.6 13.6 1.0 H28 A:MQF203 3.7 14.4 1.0 HG21 A:ILE104 3.8 11.2 1.0 C02 A:MQF203 3.9 11.9 1.0 HB3 A:CYS117 4.0 12.8 1.0 CE2 A:TYR19 4.0 9.4 1.0 CG1 A:ILE104 4.1 12.2 1.0 HG13 A:ILE104 4.2 12.5 1.0 O A:HOH371 4.2 14.6 1.0 C17 A:MQF203 4.2 15.9 1.0 F16 A:MQF203 4.2 18.2 1.0 CB A:CYS117 4.3 13.6 1.0 CE1 A:PHE16 4.4 11.1 1.0 OH A:TYR19 4.4 10.3 1.0 HG23 A:ILE104 4.4 11.3 1.0 CG2 A:ILE104 4.5 11.5 1.0 O19 A:MQF203 4.5 16.4 1.0 C12 A:MQF203 4.5 13.9 1.0 CZ A:TYR19 4.6 8.9 1.0 C06 A:MQF203 4.6 12.9 1.0 O A:HOH398 4.6 26.6 1.0 O07 A:MQF203 4.7 13.5 1.0 HG12 A:VAL115 4.7 12.2 1.0 HD11 A:ILE104 4.8 15.5 1.0 HZ A:PHE16 4.8 10.8 1.0 HD3 A:ARG126 4.8 12.5 1.0 C01 A:MQF203 4.8 12.6 1.0 HB2 A:CYS117 4.8 13.3 1.0 HG11 A:VAL115 4.8 12.5 1.0 CD2 A:TYR19 4.9 9.5 1.0 HD2 A:TYR19 4.9 9.0 1.0 CB A:ILE104 4.9 10.3 1.0 CD1 A:ILE104 4.9 16.1 1.0 C13 A:MQF203 5.0 15.9 1.0

Fluorine binding site 3 out of 6 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F203 b:21.7 occ:1.00 F11 A:MQF203 0.0 21.7 1.0 C08 A:MQF203 1.3 18.0 1.0 F10 A:MQF203 2.2 20.6 1.0 F09 A:MQF203 2.2 22.9 1.0 C04 A:MQF203 2.3 15.6 1.0 HG A:CYS117 2.6 16.6 1.0 C17 A:MQF203 2.7 15.9 1.0 C05 A:MQF203 2.8 13.6 1.0 O19 A:MQF203 3.0 16.4 1.0 HG11 A:VAL115 3.1 12.5 1.0 SG A:CYS117 3.2 17.6 1.0 HG12 A:VAL115 3.2 12.2 1.0 O18 A:MQF203 3.3 14.7 1.0 HD3 A:ARG126 3.3 12.5 1.0 N03 A:MQF203 3.5 14.4 1.0 CG1 A:VAL115 3.6 12.6 1.0 HE A:ARG126 3.7 11.9 1.0 HG21 A:ILE104 3.7 11.2 1.0 NE A:ARG126 4.0 11.9 1.0 HE1 A:PHE16 4.1 10.1 1.0 CD A:ARG126 4.1 12.5 1.0 C06 A:MQF203 4.1 12.9 1.0 HG23 A:ILE104 4.1 11.3 1.0 HG13 A:VAL115 4.2 11.8 1.0 HG12 A:ILE104 4.4 12.2 1.0 CG2 A:ILE104 4.4 11.5 1.0 HD2 A:ARG126 4.5 12.3 1.0 HB A:VAL115 4.5 10.5 1.0 C02 A:MQF203 4.6 11.9 1.0 CE1 A:PHE16 4.7 11.1 1.0 CB A:VAL115 4.7 10.9 1.0 H26 A:MQF203 4.7 14.0 1.0 HB2 A:ARG126 4.7 9.1 1.0 CB A:CYS117 4.8 13.6 1.0 HH21 A:ARG106 4.8 20.9 1.0 O A:HOH339 4.9 18.0 1.0 HH21 A:ARG126 4.9 12.6 1.0 HB3 A:CYS117 4.9 12.8 1.0 HG A:CYS124 4.9 15.2 0.2 C01 A:MQF203 4.9 12.6 1.0 HG21 A:VAL115 5.0 11.1 1.0 O A:HOH353 5.0 18.7 1.0 HG22 A:ILE104 5.0 11.3 1.0

Fluorine binding site 4 out of 6 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F203 b:18.4 occ:1.00 F14 A:MQF203 0.0 18.4 1.0 C13 A:MQF203 1.3 15.9 1.0 F15 A:MQF203 2.1 17.0 1.0 F16 A:MQF203 2.2 18.2 1.0 C12 A:MQF203 2.3 13.9 1.0 H27 A:MQF203 2.6 14.6 1.0 O07 A:MQF203 2.7 13.5 1.0 HB3 A:ASP76 3.0 13.8 1.0 HG2 A:MET20 3.2 9.8 1.0 H28 A:MQF203 3.2 14.4 1.0 OD1 A:ASP76 3.5 12.6 1.0 HB3 A:ALA75 3.6 13.0 1.0 HG21 A:VAL25 3.7 12.9 1.0 CG A:ASP76 3.7 13.3 1.0 CB A:ASP76 3.8 14.0 1.0 C02 A:MQF203 3.9 11.9 1.0 SD A:MET20 3.9 11.8 1.0 H A:ASP76 3.9 12.3 1.0 CG A:MET20 3.9 9.8 1.0 HZ A:PHE16 3.9 10.8 1.0 H30 A:MQF203 4.2 14.8 1.0 HH21 A:ARG78 4.2 11.3 1.0 N A:ASP76 4.3 12.4 1.0 H40 A:MQF203 4.3 23.5 1.0 HG3 A:MET20 4.4 10.1 1.0 HB2 A:ASP76 4.4 14.3 1.0 HG11 A:VAL25 4.5 12.2 1.0 N03 A:MQF203 4.5 14.4 1.0 HD12 A:LEU23 4.5 12.7 1.0 CZ A:PHE16 4.6 10.9 1.0 CB A:ALA75 4.6 13.4 1.0 OD2 A:ASP76 4.6 14.9 1.0 CA A:ASP76 4.6 13.7 1.0 HD13 A:LEU23 4.6 12.6 1.0 CG2 A:VAL25 4.6 13.0 1.0 HG22 A:THR29 4.7 14.9 1.0 C01 A:MQF203 4.8 12.6 1.0 C20 A:MQF203 4.8 14.2 1.0 HB1 A:ALA75 4.9 12.8 1.0 HA A:ASP76 4.9 13.5 1.0 C A:ALA75 4.9 13.2 1.0 HG23 A:VAL25 5.0 12.1 1.0 HE1 A:PHE16 5.0 10.1 1.0 HG22 A:VAL25 5.0 12.9 1.0 HB3 A:MET20 5.0 8.9 1.0 CD1 A:LEU23 5.0 12.9 1.0 NH2 A:ARG78 5.0 11.6 1.0

Fluorine binding site 5 out of 6 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F203 b:17.0 occ:1.00 F15 A:MQF203 0.0 17.0 1.0 C13 A:MQF203 1.3 15.9 1.0 F14 A:MQF203 2.1 18.4 1.0 F16 A:MQF203 2.2 18.2 1.0 C12 A:MQF203 2.3 13.9 1.0 H28 A:MQF203 2.5 14.4 1.0 H27 A:MQF203 2.5 14.6 1.0 HH21 A:ARG78 2.7 11.3 1.0 HD13 A:LEU23 2.8 12.6 1.0 HD12 A:LEU23 3.0 12.7 1.0 OD1 A:ASP76 3.1 12.6 1.0 CD1 A:LEU23 3.2 12.9 1.0 NH2 A:ARG78 3.2 11.6 1.0 HD11 A:LEU23 3.2 12.2 1.0 HH22 A:ARG78 3.3 11.2 1.0 O07 A:MQF203 3.5 13.5 1.0 HG2 A:MET20 3.5 9.8 1.0 CG A:ASP76 3.6 13.3 1.0 HE2 A:TYR19 3.6 8.9 1.0 O A:HOH371 3.7 14.6 1.0 HG21 A:VAL25 4.0 12.9 1.0 HB3 A:ASP76 4.0 13.8 1.0 OD2 A:ASP76 4.0 14.9 1.0 HE A:ARG78 4.1 11.8 1.0 CZ A:ARG78 4.3 11.0 1.0 CE2 A:TYR19 4.3 9.4 1.0 CB A:ASP76 4.4 14.0 1.0 C02 A:MQF203 4.4 11.9 1.0 N03 A:MQF203 4.4 14.4 1.0 H A:ASP76 4.5 12.3 1.0 CG A:MET20 4.5 9.8 1.0 HA A:MET20 4.5 9.1 1.0 HB A:THR74 4.6 9.3 1.0 CG A:LEU23 4.6 11.7 1.0 HG23 A:VAL25 4.7 12.1 1.0 CG2 A:VAL25 4.7 13.0 1.0 NE A:ARG78 4.7 11.8 1.0 HD2 A:TYR19 4.7 9.0 1.0 HB2 A:LEU23 4.7 11.3 1.0 HG1 A:THR74 4.8 10.7 1.0 HG3 A:MET20 4.8 10.1 1.0 O A:HOH398 4.8 26.6 1.0 HZ A:PHE16 4.9 10.8 1.0 HB3 A:ALA75 4.9 13.0 1.0 HG22 A:VAL25 4.9 12.9 1.0 HE1 A:PHE16 4.9 10.1 1.0 CD2 A:TYR19 4.9 9.5 1.0 HB3 A:LEU23 4.9 11.1 1.0 HB2 A:ASP76 5.0 14.3 1.0

Fluorine binding site 6 out of 6 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-Cyclohexyl-6-(2,2,2-Trifluoroethoxy)-2- (Trifluoromethyl)Pyridine-3-Carboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F203 b:18.2 occ:1.00 F16 A:MQF203 0.0 18.2 1.0 C13 A:MQF203 1.4 15.9 1.0 F15 A:MQF203 2.2 17.0 1.0 F14 A:MQF203 2.2 18.4 1.0 C12 A:MQF203 2.3 13.9 1.0 H28 A:MQF203 2.5 14.4 1.0 O07 A:MQF203 2.7 13.5 1.0 HZ A:PHE16 2.8 10.8 1.0 HE1 A:PHE16 2.9 10.1 1.0 HG2 A:MET20 3.0 9.8 1.0 H27 A:MQF203 3.1 14.6 1.0 HE2 A:TYR19 3.2 8.9 1.0 C02 A:MQF203 3.2 11.9 1.0 N03 A:MQF203 3.2 14.4 1.0 CZ A:PHE16 3.2 10.9 1.0 CE1 A:PHE16 3.3 11.1 1.0 HG3 A:MET20 3.6 10.1 1.0 CG A:MET20 3.7 9.8 1.0 HD2 A:TYR19 3.7 9.0 1.0 HD12 A:LEU23 3.9 12.7 1.0 CE2 A:TYR19 3.9 9.4 1.0 CD2 A:TYR19 4.2 9.5 1.0 SD A:MET20 4.2 11.8 1.0 F10 A:MQF203 4.2 20.6 1.0 C01 A:MQF203 4.3 12.6 1.0 C04 A:MQF203 4.3 15.6 1.0 HD11 A:LEU23 4.3 12.2 1.0 CE2 A:PHE16 4.4 11.3 1.0 CD1 A:LEU23 4.4 12.9 1.0 HD13 A:LEU23 4.4 12.6 1.0 H40 A:MQF203 4.5 23.5 1.0 CD1 A:PHE16 4.5 9.6 1.0 O A:HOH371 4.6 14.6 1.0 HA A:MET20 4.6 9.1 1.0 H30 A:MQF203 4.7 14.8 1.0 HE2 A:PHE16 4.7 11.0 1.0 HH21 A:ARG78 4.7 11.3 1.0 HD1 A:PHE16 4.9 9.9 1.0 C08 A:MQF203 4.9 18.0 1.0 OD1 A:ASP76 4.9 12.6 1.0 C20 A:MQF203 4.9 14.2 1.0 HG21 A:VAL25 5.0 12.9 1.0 HB3 A:ALA75 5.0 13.0 1.0 CB A:MET20 5.0 9.1 1.0

U.Obst, C.Magnone, B.Kuhn, M.G.Rudolph. Crystal Structure of A Human FABP4 Binding Site Mutated to That of FABP5 Complex To Be Published.