Chlorine in PDB 3olf: Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid

The structure of Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid, PDB code: 3olf was solved by M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.44 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	72.280, 84.860, 191.560, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 23.8

The structure of Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid (pdb code 3olf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid, PDB code: 3olf:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:35.5 occ:1.00 CL32 A:OLF1 0.0 35.5 1.0 C29 A:OLF1 1.7 33.4 1.0 C30 A:OLF1 2.7 30.2 1.0 C31 A:OLF1 2.7 32.3 1.0 CZ A:PHE333 3.9 28.8 1.0 SD A:MET454 4.0 51.9 1.0 C24 A:OLF1 4.0 30.3 1.0 C25 A:OLF1 4.0 30.8 1.0 CD2 A:LEU291 4.1 30.1 1.0 CD2 A:LEU455 4.2 33.3 1.0 CE1 A:HIS451 4.2 30.9 0.3 CZ3 A:TRP458 4.3 37.2 1.0 CE1 A:PHE333 4.3 29.1 1.0 CG A:MET454 4.4 47.0 1.0 C14 A:OLF1 4.5 28.9 1.0 CD1 A:LEU291 4.6 29.9 1.0 ND1 A:HIS451 4.6 32.3 0.3 CG A:LEU455 4.9 35.5 1.0 CE2 A:PHE333 4.9 30.3 1.0 CE A:MET332 5.0 36.0 1.0 CE3 A:TRP458 5.0 36.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Fxr in Complex with 4-({(2S)-2-[2-(4- Chlorophenyl)-5,6-Difluoro-1H-Benzimidazol-1-Yl]-2- Cyclohexylacetyl}Amino)-3-Methylbenzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl2 b:43.4 occ:1.00 CL32 C:OLF2 0.0 43.4 1.0 C29 C:OLF2 1.7 38.9 1.0 C30 C:OLF2 2.7 39.0 1.0 C31 C:OLF2 2.7 37.1 1.0 CZ C:PHE333 3.9 38.5 1.0 C24 C:OLF2 4.0 38.7 1.0 C25 C:OLF2 4.0 34.4 1.0 CG C:MET454 4.1 50.2 1.0 CZ3 C:TRP458 4.1 41.9 1.0 SD C:MET454 4.1 54.6 1.0 CE1 C:PHE333 4.2 40.2 1.0 CD2 C:LEU455 4.3 45.5 1.0 CD1 C:ILE361 4.4 51.7 1.0 CE C:MET332 4.4 43.5 1.0 CD2 C:LEU291 4.4 39.4 1.0 C14 C:OLF2 4.5 33.5 1.0 CG C:LEU455 4.7 44.0 1.0 CD1 C:LEU291 4.7 34.7 1.0 CE3 C:TRP458 4.9 41.0 1.0 CE2 C:PHE333 4.9 40.2 1.0 CH2 C:TRP458 5.0 42.5 1.0

H.G.F.Richter, G.M.Benson, K.H.Bleicher, D.Blum, E.Chaput, N.Clemann, S.Feng, C.Gardes, U.Grether, P.Hartman, B.Kuhn, R.E.Martin, J.M.Plancher, M.G.Rudolph, F.Schuler, S.Taylor. Optimization of A Novel Class of Benzimidazole-Based Farnesoid X Receptor (Fxr) Agonists to Improve Physicochemical and Adme Properties Bioorg.Med.Chem.Lett. V. 21 1134 2011.
ISSN: ISSN 0960-894X
PubMed: 21269824
DOI: 10.1016/J.BMCL.2010.12.123