Fluorine in PDB 5u45: Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14

The structure of Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14, PDB code: 5u45 was solved by C.-C.Wu, T.J.Baiga, M.Downes, J.J.La Clair, A.R.Atkins, S.B.Richard, T.A.Stockley-Noel, M.E.Bowman, R.M.Evans, J.P.Noel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.80 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.530, 95.260, 96.440, 90.00, 97.56, 90.00
R / Rfree (%)	19 / 24.1

The binding sites of Fluorine atom in the Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14 (pdb code 5u45). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14, PDB code: 5u45:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14 within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:31.3 occ:1.00 F A:7SY502 0.0 31.3 1.0 C28 A:7SY502 1.3 37.4 1.0 C27 A:7SY502 2.4 32.0 1.0 C24 A:7SY502 2.4 32.5 1.0 HE2 A:PHE316 2.6 49.6 1.0 H25 A:7SY502 2.6 39.0 1.0 H28 A:7SY502 2.6 38.4 1.0 HG11 A:VAL312 2.7 47.2 1.0 HG22 A:VAL245 2.9 37.5 1.0 HG13 A:VAL245 3.0 29.0 1.0 HD21 A:LEU317 3.1 42.6 1.0 HG21 A:VAL312 3.3 39.3 1.0 HG13 A:VAL312 3.3 47.2 1.0 HD2 A:PHE316 3.4 47.2 1.0 CE2 A:PHE316 3.4 41.3 1.0 HG21 A:VAL245 3.4 37.5 1.0 HD23 A:LEU317 3.4 42.6 1.0 CG1 A:VAL312 3.5 39.4 1.0 HG11 A:VAL245 3.5 29.0 1.0 CG2 A:VAL245 3.6 31.3 1.0 CG1 A:VAL245 3.6 24.2 1.0 C26 A:7SY502 3.6 31.8 1.0 C21 A:7SY502 3.6 31.6 1.0 CD2 A:LEU317 3.7 35.5 1.0 CD2 A:PHE316 3.8 39.3 1.0 HG22 A:VAL312 3.8 39.3 1.0 CG2 A:VAL312 3.9 32.7 1.0 HD13 A:LEU219 4.0 51.8 1.0 HG21 A:ILE213 4.0 40.1 1.0 C25 A:7SY502 4.1 32.1 1.0 HG12 A:VAL312 4.2 47.2 1.0 HD22 A:LEU317 4.2 42.6 1.0 CB A:VAL245 4.2 27.6 1.0 CB A:VAL312 4.3 29.9 1.0 HG23 A:VAL245 4.4 37.5 1.0 HD22 A:LEU219 4.4 63.8 1.0 HG22 A:ILE213 4.4 40.1 1.0 HG12 A:VAL245 4.4 29.0 1.0 H27 A:7SY502 4.5 38.1 1.0 H20 A:7SY502 4.5 34.5 1.0 HA A:VAL245 4.5 24.7 1.0 CZ A:PHE316 4.6 36.8 1.0 HD11 A:LEU320 4.7 37.8 1.0 CG2 A:ILE213 4.7 33.4 1.0 HB A:VAL312 4.7 35.9 1.0 HZ A:PHE316 4.7 44.1 1.0 HG A:LEU317 4.8 40.6 1.0 HG23 A:VAL312 4.8 39.3 1.0 CG A:LEU317 4.9 33.8 1.0 CD1 A:LEU219 4.9 43.1 1.0 C19 A:7SY502 4.9 26.8 1.0 HB A:VAL245 5.0 33.1 1.0 CA A:VAL245 5.0 20.6 1.0 HD11 A:LEU219 5.0 51.8 1.0 HD13 A:ILE213 5.0 37.6 1.0

Fluorine binding site 2 out of 2 in the Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 14 within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:32.1 occ:1.00 F B:7SY502 0.0 32.1 1.0 C28 B:7SY502 1.3 24.2 1.0 C27 B:7SY502 2.4 16.6 1.0 C24 B:7SY502 2.4 20.0 1.0 HE2 B:PHE316 2.5 37.7 1.0 H28 B:7SY502 2.6 19.9 1.0 H25 B:7SY502 2.6 24.0 1.0 HG22 B:VAL245 2.6 28.3 1.0 HG13 B:VAL245 2.9 37.9 1.0 HG11 B:VAL312 2.9 29.3 1.0 HG21 B:VAL245 3.1 28.3 1.0 HD21 B:LEU317 3.1 27.7 1.0 CG2 B:VAL245 3.3 23.6 1.0 HG11 B:VAL245 3.3 37.9 1.0 CE2 B:PHE316 3.4 31.4 1.0 CG1 B:VAL245 3.5 31.6 1.0 HD23 B:LEU317 3.5 27.7 1.0 HG13 B:VAL312 3.5 29.3 1.0 HD2 B:PHE316 3.6 41.5 1.0 HG21 B:VAL312 3.6 28.8 1.0 C26 B:7SY502 3.6 24.3 1.0 C21 B:7SY502 3.6 19.0 1.0 CG1 B:VAL312 3.7 24.4 1.0 HD13 B:LEU219 3.7 46.1 1.0 CD2 B:LEU317 3.8 23.1 1.0 CD2 B:PHE316 3.9 34.6 1.0 CB B:VAL245 4.0 26.0 1.0 HG21 B:ILE213 4.1 35.5 1.0 HG23 B:VAL245 4.1 28.3 1.0 C25 B:7SY502 4.1 25.3 1.0 HG22 B:VAL312 4.1 28.8 1.0 CG2 B:VAL312 4.2 24.0 1.0 HD22 B:LEU317 4.3 27.7 1.0 HG12 B:VAL312 4.3 29.3 1.0 HG12 B:VAL245 4.4 37.9 1.0 HA B:VAL245 4.4 24.3 1.0 HD11 B:LEU320 4.4 33.9 1.0 H27 B:7SY502 4.5 29.2 1.0 CZ B:PHE316 4.5 36.9 1.0 HG22 B:ILE213 4.5 35.5 1.0 H20 B:7SY502 4.5 31.6 1.0 CD1 B:LEU219 4.6 38.4 1.0 CB B:VAL312 4.6 25.2 1.0 HD11 B:LEU219 4.6 46.1 1.0 HD22 B:LEU219 4.6 44.9 1.0 HZ B:PHE316 4.6 44.3 1.0 HB B:VAL245 4.7 31.2 1.0 CG2 B:ILE213 4.8 29.6 1.0 CA B:VAL245 4.8 20.3 1.0 HG B:LEU317 4.8 30.7 1.0 C19 B:7SY502 4.9 22.1 1.0 HB B:VAL312 4.9 30.3 1.0 CG B:LEU317 5.0 25.6 1.0

C.C.Wu, T.J.Baiga, M.Downes, J.J.La Clair, A.R.Atkins, S.B.Richard, W.Fan, T.A.Stockley-Noel, M.E.Bowman, J.P.Noel, R.M.Evans. Structural Basis For Specific Ligation of the Peroxisome Proliferator-Activated Receptor Delta. Proc. Natl. Acad. Sci. V. 114 E2563 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28320959
DOI: 10.1073/PNAS.1621513114