Chlorine in PDB 3rut: Fxr with SRC1 and GSK359

All present enzymatic activity of Fxr with SRC1 and GSK359:
2.3.1.48;

The structure of Fxr with SRC1 and GSK359, PDB code: 3rut was solved by S.P.Williams, K.P.Madauss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.67 / 3.00
Space group	F 2 3
Cell size a, b, c (Å), α, β, γ (°)	158.274, 158.274, 158.274, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 26.6

The binding sites of Chlorine atom in the Fxr with SRC1 and GSK359 (pdb code 3rut). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Fxr with SRC1 and GSK359, PDB code: 3rut:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Fxr with SRC1 and GSK359


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fxr with SRC1 and GSK359 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:47.8 occ:1.00 CL31 A:59G1 0.0 47.8 1.0 C30 A:59G1 1.8 46.0 1.0 C32 A:59G1 2.7 46.0 1.0 C29 A:59G1 2.7 44.9 1.0 C07 A:59G1 3.0 44.0 1.0 C08 A:59G1 3.5 42.8 1.0 N06 A:59G1 3.7 44.7 1.0 CD1 A:ILE357 3.8 35.0 1.0 C09 A:59G1 3.9 41.2 1.0 C33 A:59G1 4.0 45.8 1.0 C35 A:59G1 4.0 44.7 1.0 CE A:MET450 4.2 40.0 1.0 CG2 A:ILE352 4.2 31.8 1.0 SD A:MET365 4.3 44.5 1.0 C04 A:59G1 4.3 44.2 1.0 CG1 A:ILE352 4.3 31.8 1.0 O05 A:59G1 4.4 45.3 1.0 CD1 A:ILE352 4.4 31.0 1.0 O10 A:59G1 4.5 39.6 1.0 C34 A:59G1 4.5 45.0 1.0 CE A:MET365 4.7 43.5 1.0 CB A:ILE352 4.9 32.0 1.0 CH2 A:TRP454 5.0 38.5 1.0

Chlorine binding site 2 out of 2 in the Fxr with SRC1 and GSK359


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Fxr with SRC1 and GSK359 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:44.3 occ:1.00 CL36 A:59G1 0.0 44.3 1.0 C35 A:59G1 1.7 44.7 1.0 C34 A:59G1 2.7 45.0 1.0 C29 A:59G1 2.7 44.9 1.0 C07 A:59G1 2.9 44.0 1.0 N06 A:59G1 3.4 44.7 1.0 SD A:MET328 3.4 37.6 1.0 CB A:MET328 3.6 37.0 1.0 O10 A:59G1 3.6 39.6 1.0 C08 A:59G1 3.7 42.8 1.0 CH2 A:TRP469 3.9 38.9 1.0 CZ2 A:TRP469 3.9 38.6 1.0 C33 A:59G1 3.9 45.8 1.0 C30 A:59G1 4.0 46.0 1.0 NE2 A:HIS447 4.0 42.4 1.0 CG A:MET328 4.1 37.4 1.0 O05 A:59G1 4.3 45.3 1.0 C09 A:59G1 4.3 41.2 1.0 C04 A:59G1 4.4 44.2 1.0 O A:VAL325 4.5 36.2 1.0 C32 A:59G1 4.5 46.0 1.0 CG2 A:VAL325 4.5 36.1 1.0 CD2 A:HIS447 4.5 42.5 1.0 C11 A:59G1 4.5 37.4 1.0 CA A:VAL325 4.6 36.3 1.0 C12 A:59G1 4.7 36.7 1.0 CE1 A:HIS447 4.8 42.4 1.0 CA A:MET328 4.9 36.9 1.0 CB A:VAL325 5.0 36.3 1.0

A.Akwabi-Ameyaw, J.A.Caravella, L.Chen, K.L.Creech, D.N.Deaton, K.P.Madauss, H.B.Marr, A.B.Miller, F.Navas, D.J.Parks, P.K.Spearing, D.Todd, S.P.Williams, G.B.Wisely. Conformationally Constrained Farnesoid X Receptor (Fxr) Agonists: Alternative Replacements of the Stilbene. Bioorg.Med.Chem.Lett. V. 21 6154 2011.
ISSN: ISSN 0960-894X
PubMed: 21890356
DOI: 10.1016/J.BMCL.2011.08.034