Bromine in PDB 7fym: Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid

The structure of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid, PDB code: 7fym was solved by A.Ehler, J.Benz, U.Obst, P.Mohr, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.26 / 1.21
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.259, 53.007, 72.387, 90, 90, 90
R / Rfree (%)	16.5 / 20.7

The binding sites of Bromine atom in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid (pdb code 7fym). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid, PDB code: 7fym:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Br201 b:17.9 occ:0.50 BR11 A:W8N201 0.0 17.9 0.5 H34 A:W8N201 0.8 17.7 0.5 C15 A:W8N201 1.4 17.1 0.5 H32 A:W8N201 1.8 17.6 0.5 C10 A:W8N201 1.9 18.8 0.5 C07 A:W8N201 1.9 14.7 0.5 C07 A:W8N201 2.0 27.3 0.5 BR11 A:W8N201 2.1 38.1 0.5 H33 A:W8N201 2.2 17.6 0.5 H34 A:W8N201 2.8 17.1 0.5 C03 A:W8N201 2.8 16.4 0.5 H19 A:W8N201 2.9 16.4 0.5 C10 A:W8N201 2.9 15.7 0.5 C15 A:W8N201 3.1 16.6 0.5 HG3 A:PRO38 3.2 13.5 1.0 HB1 A:ALA36 3.2 15.9 1.0 H32 A:W8N201 3.2 17.2 0.5 C08 A:W8N201 3.3 22.6 0.5 C03 A:W8N201 3.3 20.9 0.5 HB3 A:PRO38 3.4 11.1 1.0 HB3 A:SER55 3.4 11.3 1.0 HB3 A:ALA36 3.5 17.1 1.0 HG A:SER55 3.5 12.5 1.0 OG A:SER55 3.6 12.8 1.0 HD3 A:PRO38 3.6 11.3 1.0 CB A:ALA36 3.7 16.6 1.0 H23 A:W8N201 3.7 20.7 0.5 H19 A:W8N201 3.9 21.9 0.5 HB2 A:ALA36 3.9 17.1 1.0 CG A:PRO38 3.9 14.9 1.0 CB A:SER55 3.9 11.7 1.0 C4 A:PG4202 4.0 32.6 1.0 H33 A:W8N201 4.1 17.4 0.5 CB A:PRO38 4.1 11.0 1.0 C01 A:W8N201 4.1 15.8 0.5 C08 A:W8N201 4.2 13.8 0.5 HG22 A:THR53 4.2 15.8 1.0 HB2 A:SER55 4.2 11.8 1.0 C04 A:W8N201 4.2 23.4 0.5 C01 A:W8N201 4.2 22.5 0.5 CD A:PRO38 4.3 11.1 1.0 HB3 A:LYS58 4.4 13.8 1.0 C5 A:PG4202 4.4 35.0 1.0 HA2 A:GLY33 4.5 14.9 1.0 C04 A:W8N201 4.7 17.8 0.5 HB2 A:PRO38 4.7 10.8 1.0 HH22 A:ARG126 4.7 14.2 1.0 O3 A:PG4202 4.7 38.4 1.0 HG2 A:PRO38 4.8 14.0 1.0 HG21 A:THR53 4.8 15.6 1.0 O A:LYS58 4.8 9.4 1.0 O A:HOH330 4.9 16.1 1.0 CG2 A:THR53 4.9 15.9 1.0 H23 A:W8N201 4.9 14.9 0.5

Bromine binding site 2 out of 2 in the Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Human FABP4 Binding Site Mutated to That of FABP5 in Complex with 5-(3-Bromo-4-Methylphenyl)-3,3-Dimethyl-5- Oxopentanoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Br201 b:38.1 occ:0.50 BR11 A:W8N201 0.0 38.1 0.5 C07 A:W8N201 1.9 27.3 0.5 BR11 A:W8N201 2.1 17.9 0.5 H19 A:W8N201 2.1 16.4 0.5 H19 A:W8N201 2.7 21.9 0.5 C03 A:W8N201 2.7 20.9 0.5 C03 A:W8N201 2.7 16.4 0.5 C07 A:W8N201 2.8 14.7 0.5 H34 A:W8N201 2.8 17.7 0.5 HB3 A:ALA36 2.9 17.1 1.0 C10 A:W8N201 2.9 18.8 0.5 C15 A:W8N201 3.2 17.1 0.5 HA2 A:GLY33 3.3 14.9 1.0 H32 A:W8N201 3.3 17.6 0.5 O A:HOH330 3.4 16.1 1.0 HE2 A:PHE16 3.4 10.4 1.0 HB1 A:ALA36 3.6 15.9 1.0 HG3 A:PRO38 3.6 13.5 1.0 HH22 A:ARG126 3.6 14.2 1.0 C5 A:PG4202 3.6 35.0 1.0 CB A:ALA36 3.6 16.6 1.0 O A:GLY33 3.6 17.8 1.0 HD3 A:PRO38 3.8 11.3 1.0 HB2 A:ALA36 3.9 17.1 1.0 HZ A:PHE16 3.9 11.1 1.0 C01 A:W8N201 4.0 15.8 0.5 C01 A:W8N201 4.0 22.5 0.5 HA3 A:GLY33 4.0 15.3 1.0 CA A:GLY33 4.0 14.8 1.0 C4 A:PG4202 4.0 32.6 1.0 NH2 A:ARG126 4.0 14.7 1.0 C10 A:W8N201 4.1 15.7 0.5 CE2 A:PHE16 4.1 10.6 1.0 H33 A:W8N201 4.1 17.6 0.5 O06 A:W8N201 4.2 20.2 0.5 HH21 A:ARG126 4.2 14.1 1.0 C08 A:W8N201 4.2 22.6 0.5 C A:GLY33 4.3 14.1 1.0 CZ A:PHE16 4.4 11.2 1.0 O3 A:PG4202 4.4 38.4 1.0 CG A:PRO38 4.4 14.9 1.0 CD A:PRO38 4.5 11.1 1.0 C02 A:W8N201 4.6 17.7 0.5 C04 A:W8N201 4.6 23.4 0.5 O4 A:PG4202 4.6 30.5 1.0 H34 A:W8N201 4.7 17.1 0.5 H32 A:W8N201 4.7 17.2 0.5 HB3 A:PRO38 4.7 11.1 1.0 C15 A:W8N201 4.8 16.6 0.5 C6 A:PG4202 4.8 26.6 1.0 O06 A:W8N201 4.8 30.4 0.5 CA A:ALA36 4.9 17.1 1.0 HD2 A:PRO38 4.9 11.2 1.0 H A:ALA36 4.9 19.8 1.0 C02 A:W8N201 4.9 25.0 0.5 HH12 A:ARG126 4.9 12.2 1.0 C04 A:W8N201 5.0 17.8 0.5 H23 A:W8N201 5.0 20.7 0.5

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.