Chlorine in PDB 7sqb: Ppar Gamma Lbd Bound to Inverse Agonist SR10221

The structure of Ppar Gamma Lbd Bound to Inverse Agonist SR10221, PDB code: 7sqb was solved by R.L.Frkic, J.L.Pederick, J.B.Bruning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.30 / 2.60
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	65.854, 65.854, 363.331, 90, 90, 120
R / Rfree (%)	22.5 / 26.1

The binding sites of Chlorine atom in the Ppar Gamma Lbd Bound to Inverse Agonist SR10221 (pdb code 7sqb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Ppar Gamma Lbd Bound to Inverse Agonist SR10221, PDB code: 7sqb:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Ppar Gamma Lbd Bound to Inverse Agonist SR10221


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ppar Gamma Lbd Bound to Inverse Agonist SR10221 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:166.9 occ:0.94 CL40 A:A8R501 0.0 166.9 0.9 C16 A:A8R501 1.8 130.6 0.9 C17 A:A8R501 2.8 114.0 0.9 C15 A:A8R501 2.8 129.6 0.9 O19 A:A8R501 3.0 126.3 0.9 CG2 A:ILE326 3.5 89.7 1.0 CA A:SER289 3.5 76.7 1.0 CD1 A:ILE326 3.6 114.4 1.0 CG1 A:ILE326 3.6 93.7 1.0 OG A:SER289 3.7 128.7 1.0 CB A:ALA292 3.8 93.4 1.0 CB A:SER289 3.9 97.8 1.0 C18 A:A8R501 4.1 98.1 0.9 C14 A:A8R501 4.1 114.3 0.9 N A:SER289 4.1 95.4 1.0 CB A:ILE326 4.2 87.9 1.0 O A:ARG288 4.3 83.6 1.0 C20 A:A8R501 4.4 132.0 0.9 O22 A:A8R501 4.4 142.6 0.9 C A:ARG288 4.5 92.5 1.0 C13 A:A8R501 4.6 88.8 0.9 C A:SER289 4.6 92.5 1.0 O A:SER289 4.6 93.2 1.0 C21 A:A8R501 4.8 136.6 0.9 CG A:ARG288 4.9 87.4 1.0 CA A:ILE326 5.0 85.4 1.0

Chlorine binding site 2 out of 2 in the Ppar Gamma Lbd Bound to Inverse Agonist SR10221


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ppar Gamma Lbd Bound to Inverse Agonist SR10221 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:203.1 occ:0.95 CL40 A:A8R502 0.0 203.1 0.9 C16 A:A8R502 1.8 199.3 0.9 C15 A:A8R502 2.7 185.3 0.9 C17 A:A8R502 2.8 208.5 0.9 O19 A:A8R502 3.0 219.3 0.9 O22 A:A8R502 3.3 211.6 0.9 C39 A:A8R502 3.5 204.9 0.9 C20 A:A8R502 3.6 213.3 0.9 NE2 A:HIS266 3.6 197.6 1.0 C21 A:A8R502 3.8 210.9 0.9 CE1 A:HIS266 3.8 196.7 1.0 CG2 A:ILE279 4.0 103.4 0.7 CD2 A:LEU270 4.0 147.6 1.0 C14 A:A8R502 4.0 178.4 0.9 OE1 A:GLN283 4.1 155.5 1.0 C18 A:A8R502 4.1 196.0 0.9 OD2 A:ASP462 4.5 152.3 1.0 CD2 A:HIS266 4.6 195.3 1.0 C13 A:A8R502 4.6 177.7 0.9 ND1 A:HIS266 4.8 193.2 1.0 CB A:ILE279 4.8 117.8 1.0 O23 A:A8R502 4.9 205.3 0.9 CD A:GLN283 5.0 140.4 1.0

R.L.Frkic, J.L.Pederick, A.Horsfall, B.Jovcevski, E.Bruning, P.Nair, H.Rajapaksha, T.Pukala, M.Chang, B.Pascal, T.Kamenecka, J.Harmer, P.Griffin, J.B.Bruning. Ppargama Corepression Involves Alternate Ligand Conformation and Inflation of H12 Ensembles Acs Chem.Biol. 2023.
ISSN: ESSN 1554-8937
DOI: 10.1021/ACSCHEMBIO.2C00917