Chlorine in PDB 3p89: Fxr Bound to A Quinolinecarboxylic Acid

All present enzymatic activity of Fxr Bound to A Quinolinecarboxylic Acid:
2.3.1.48;

The structure of Fxr Bound to A Quinolinecarboxylic Acid, PDB code: 3p89 was solved by K.P.Madauss, S.P.Williams, D.N.Deaton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.22 / 2.30
Space group	F 2 3
Cell size a, b, c (Å), α, β, γ (°)	159.911, 159.911, 159.911, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 25.5

The binding sites of Chlorine atom in the Fxr Bound to A Quinolinecarboxylic Acid (pdb code 3p89). 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 Bound to A Quinolinecarboxylic Acid, PDB code: 3p89:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Fxr Bound to A Quinolinecarboxylic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fxr Bound to A Quinolinecarboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:44.4 occ:1.00 CL32 A:89P1 0.0 44.4 1.0 C31 A:89P1 1.8 42.5 1.0 C30 A:89P1 2.7 41.6 1.0 C33 A:89P1 2.8 41.8 1.0 C7 A:89P1 3.0 40.6 1.0 C8 A:89P1 3.4 40.0 1.0 C9 A:89P1 3.7 39.8 1.0 N6 A:89P1 3.8 40.3 1.0 CD1 A:ILE357 3.8 35.7 1.0 CG2 A:ILE352 3.9 31.3 1.0 CG1 A:ILE352 4.0 30.4 1.0 C36 A:89P1 4.0 42.0 1.0 C34 A:89P1 4.1 41.7 1.0 O10 A:89P1 4.3 39.2 1.0 CD1 A:ILE352 4.3 31.2 1.0 CE A:MET365 4.3 36.7 1.0 C4 A:89P1 4.4 39.7 1.0 CD1 A:LEU287 4.4 32.9 1.0 SD A:MET365 4.4 38.0 1.0 O5 A:89P1 4.5 40.2 1.0 CB A:ILE352 4.5 30.8 1.0 C35 A:89P1 4.6 41.9 1.0 CD2 A:LEU287 5.0 31.3 1.0

Chlorine binding site 2 out of 2 in the Fxr Bound to A Quinolinecarboxylic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Fxr Bound to A Quinolinecarboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:43.1 occ:1.00 CL37 A:89P1 0.0 43.1 1.0 C36 A:89P1 1.8 42.0 1.0 C35 A:89P1 2.7 41.9 1.0 C30 A:89P1 2.7 41.6 1.0 C7 A:89P1 3.0 40.6 1.0 N6 A:89P1 3.5 40.3 1.0 NE2 A:HIS447 3.5 38.6 1.0 SD A:MET328 3.6 44.9 1.0 CD2 A:HIS447 3.8 38.9 1.0 O10 A:89P1 3.8 39.2 1.0 CB A:MET328 3.9 38.3 1.0 C8 A:89P1 3.9 40.0 1.0 CZ2 A:TRP469 3.9 45.1 1.0 C31 A:89P1 4.0 42.5 1.0 C34 A:89P1 4.0 41.7 1.0 CH2 A:TRP469 4.3 44.9 1.0 CE1 A:HIS447 4.3 39.0 1.0 CG A:MET328 4.3 40.8 1.0 O5 A:89P1 4.4 40.2 1.0 C9 A:89P1 4.5 39.8 1.0 C33 A:89P1 4.5 41.8 1.0 C4 A:89P1 4.6 39.7 1.0 CE1 A:PHE329 4.6 41.2 1.0 O A:VAL325 4.7 38.5 1.0 CG1 A:VAL325 4.7 38.9 1.0 CA A:VAL325 4.8 39.2 1.0 CG A:HIS447 4.8 40.0 1.0 C11 A:89P1 4.8 38.5 1.0 CD1 A:PHE329 4.8 40.7 1.0 C12 A:89P1 4.9 38.5 1.0 CE2 A:TRP469 5.0 45.9 1.0

J.Y.Bass, J.A.Caravella, L.Chen, K.L.Creech, D.N.Deaton, K.P.Madauss, H.B.Marr, R.B.Mcfadyen, A.B.Miller, W.Y.Mills, F.Navas, D.J.Parks, T.L.Smalley, P.K.Spearing, D.Todd, S.P.Williams, G.B.Wisely. Conformationally Constrained Farnesoid X Receptor (Fxr) Agonists: Heteroaryl Replacements of the Naphthalene. Bioorg.Med.Chem.Lett. V. 21 1206 2011.
ISSN: ISSN 0960-894X
PubMed: 21256005
DOI: 10.1016/J.BMCL.2010.12.089