Chlorine in PDB 6a5x: Fxr-Lbd with HNC180 and SRC1

The structure of Fxr-Lbd with HNC180 and SRC1, PDB code: 6a5x was solved by N.Wang, J.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.60
Space group	F 2 3
Cell size a, b, c (Å), α, β, γ (°)	160.350, 160.350, 160.350, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 25.1

The binding sites of Chlorine atom in the Fxr-Lbd with HNC180 and SRC1 (pdb code 6a5x). 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-Lbd with HNC180 and SRC1, PDB code: 6a5x:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Fxr-Lbd with HNC180 and SRC1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fxr-Lbd with HNC180 and SRC1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:60.1 occ:1.00 CL1 A:9R3505 0.0 60.1 1.0 C13 A:9R3505 1.8 46.1 1.0 C5 A:9R3505 2.7 50.6 1.0 C12 A:9R3505 2.8 42.1 1.0 C3 A:9R3505 3.0 47.2 1.0 C2 A:9R3505 3.5 40.5 1.0 N1 A:9R3505 3.7 44.5 1.0 C6 A:9R3505 3.8 41.6 1.0 CD1 A:ILE357 4.0 39.1 1.0 C9 A:9R3505 4.0 43.4 1.0 C11 A:9R3505 4.1 41.3 1.0 CG2 A:ILE352 4.1 34.0 1.0 CG1 A:ILE352 4.2 33.0 1.0 CE A:MET450 4.3 45.3 1.0 C1 A:9R3505 4.4 42.0 1.0 CD1 A:ILE352 4.4 33.5 1.0 CD1 A:LEU287 4.4 37.5 1.0 O1 A:9R3505 4.4 41.3 1.0 C10 A:9R3505 4.6 39.4 1.0 O2 A:9R3505 4.6 39.7 1.0 SD A:MET365 4.6 62.3 1.0 CB A:ILE352 4.7 34.0 1.0 CH2 A:TRP454 4.8 33.5 1.0 C19 A:9R3505 4.8 38.1 1.0 CE A:MET365 4.8 55.8 1.0

Chlorine binding site 2 out of 2 in the Fxr-Lbd with HNC180 and SRC1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Fxr-Lbd with HNC180 and SRC1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:51.5 occ:1.00 CL2 A:9R3505 0.0 51.5 1.0 C9 A:9R3505 1.8 43.4 1.0 C10 A:9R3505 2.7 39.4 1.0 C5 A:9R3505 2.8 50.6 1.0 C3 A:9R3505 3.0 47.2 1.0 N1 A:9R3505 3.5 44.5 1.0 CE1 A:HIS447 3.6 36.6 1.0 CB A:MET328 3.7 44.7 1.0 CZ2 A:TRP469 3.7 49.8 1.0 CE A:MET328 3.7 53.7 1.0 C2 A:9R3505 3.9 40.5 1.0 O2 A:9R3505 3.9 39.7 1.0 SD A:MET328 3.9 50.9 1.0 C11 A:9R3505 4.0 41.3 1.0 C13 A:9R3505 4.0 46.1 1.0 ND1 A:HIS447 4.1 40.0 1.0 CH2 A:TRP469 4.3 47.3 1.0 O1 A:9R3505 4.3 41.3 1.0 CG A:MET328 4.3 48.1 1.0 NE2 A:HIS447 4.4 40.2 1.0 C6 A:9R3505 4.5 41.6 1.0 C12 A:9R3505 4.6 42.1 1.0 C22 A:9R3505 4.6 39.5 1.0 C1 A:9R3505 4.6 42.0 1.0 CE2 A:TRP469 4.6 48.1 1.0 CE1 A:PHE329 4.7 50.9 1.0 C20 A:9R3505 4.7 35.9 1.0 CD1 A:PHE329 4.7 50.3 1.0 O A:VAL325 4.9 47.7 1.0 C17 A:9R3505 4.9 38.0 1.0 CA A:VAL325 4.9 37.3 1.0 NE1 A:TRP469 4.9 50.9 1.0 CA A:MET328 4.9 44.1 1.0

N.Wang, Q.Zou, J.Xu, J.Zhang, J.Liu. Ligand Binding and Heterodimerization with Retinoid X Receptor Alpha (Rxr Alpha ) Induce Farnesoid X Receptor (Fxr) Conformational Changes Affecting Coactivator Binding J. Biol. Chem. V. 293 18180 2018.
ISSN: ESSN 1083-351X
PubMed: 30275017
DOI: 10.1074/JBC.RA118.004652