Chlorine in PDB 3omm: 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-Fluorobenzoic 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-Fluorobenzoic Acid, PDB code: 3omm 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)	47.62 / 2.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	72.130, 83.940, 190.480, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 25.6

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-Fluorobenzoic Acid also contains other interesting chemical elements:

Fluorine

(F)

6 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-Fluorobenzoic Acid (pdb code 3omm). 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-Fluorobenzoic Acid, PDB code: 3omm:
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-Fluorobenzoic 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-Fluorobenzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:45.5 occ:1.00 CL33 A:OMM1 0.0 45.5 1.0 C30 A:OMM1 1.7 42.9 1.0 C32 A:OMM1 2.7 42.6 1.0 C31 A:OMM1 2.7 38.7 1.0 CD2 A:LEU455 3.8 48.8 1.0 CZ A:PHE333 3.9 39.8 1.0 C24 A:OMM1 4.0 40.7 1.0 C25 A:OMM1 4.0 39.3 1.0 CB A:MET454 4.2 53.3 1.0 CD2 A:LEU291 4.3 40.0 1.0 CE1 A:PHE333 4.3 39.8 1.0 SD A:MET454 4.3 63.0 1.0 CH2 A:TRP473 4.3 55.0 1.0 CZ3 A:TRP473 4.4 54.1 1.0 CD1 A:LEU291 4.4 37.2 1.0 CZ3 A:TRP458 4.5 45.7 1.0 C14 A:OMM1 4.5 37.2 1.0 CE A:MET369 4.8 55.3 1.0 CG A:MET454 4.8 57.6 1.0 CE2 A:PHE333 4.9 42.2 1.0 C A:MET454 4.9 51.0 1.0 CG A:LEU455 4.9 50.4 1.0 O A:MET454 4.9 49.9 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-Fluorobenzoic 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-Fluorobenzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl2 b:54.0 occ:1.00 CL33 C:OMM2 0.0 54.0 1.0 C30 C:OMM2 1.7 47.0 1.0 C31 C:OMM2 2.7 46.4 1.0 C32 C:OMM2 2.7 47.1 1.0 CZ C:PHE333 3.7 50.5 1.0 C25 C:OMM2 4.0 43.9 1.0 C24 C:OMM2 4.0 46.0 1.0 CE1 C:PHE333 4.2 51.0 1.0 CD2 C:LEU455 4.2 59.8 1.0 CG C:MET454 4.3 67.4 1.0 CD1 C:ILE361 4.3 55.4 1.0 CZ3 C:TRP458 4.4 50.1 1.0 CE C:MET454 4.5 67.7 1.0 CD1 C:LEU291 4.5 52.9 1.0 C14 C:OMM2 4.5 41.8 1.0 SD C:MET454 4.6 71.4 1.0 CD2 C:LEU291 4.8 48.1 1.0 CE2 C:PHE333 4.8 52.5 1.0 CG C:LEU291 4.8 51.4 1.0 CG C:LEU455 4.8 60.4 1.0 CB C:MET454 4.8 63.4 1.0 CE C:MET332 4.8 60.3 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