Fluorine in PDB 5u44: Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 13

The structure of Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 13, PDB code: 5u44 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)	95.32 / 2.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.570, 95.410, 96.180, 90.00, 97.65, 90.00
R / Rfree (%)	19.9 / 25.3

The binding sites of Fluorine atom in the Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 13 (pdb code 5u44). 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 13, PDB code: 5u44:
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 13


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 13 within 5.0Å range: probe atom residue distance (Å) B Occ A:F504 b:0.5 occ:1.00 F30 A:7SV504 0.0 0.5 1.0 C29 A:7SV504 1.4 93.8 1.0 H311 A:7SV504 2.2 60.0 1.0 HG13 A:VAL245 2.3 52.8 1.0 C28 A:7SV504 2.4 89.5 1.0 C24 A:7SV504 2.4 73.5 1.0 HD21 A:LEU317 2.5 42.3 1.0 H281 A:7SV504 2.5 0.4 1.0 C31 A:7SV504 2.8 50.0 1.0 C23 A:7SV504 2.9 49.7 1.0 CG1 A:VAL245 3.1 44.0 1.0 HG11 A:VAL312 3.2 47.0 1.0 HG11 A:VAL245 3.2 52.8 1.0 CD2 A:LEU317 3.3 35.2 1.0 HG12 A:VAL245 3.4 52.8 1.0 HD22 A:LEU317 3.4 42.3 1.0 HG21 A:VAL312 3.4 41.4 1.0 C27 A:7SV504 3.6 83.9 1.0 C25 A:7SV504 3.7 80.6 1.0 HD23 A:LEU317 3.7 42.3 1.0 HG A:CYS249 3.8 48.2 1.0 C32 A:7SV504 4.0 37.7 1.0 HD11 A:LEU317 4.1 42.7 1.0 CG1 A:VAL312 4.2 39.1 1.0 C26 A:7SV504 4.2 81.3 1.0 HG22 A:VAL245 4.2 58.4 1.0 C22 A:7SV504 4.2 37.8 1.0 CB A:VAL245 4.3 45.0 1.0 CG2 A:VAL312 4.3 34.5 1.0 HA A:VAL245 4.4 47.8 1.0 H321 A:7SV504 4.4 45.3 1.0 H271 A:7SV504 4.4 0.7 1.0 H251 A:7SV504 4.4 96.7 1.0 HG11 A:VAL305 4.5 41.5 1.0 HB A:VAL312 4.5 45.5 1.0 CG A:LEU317 4.5 28.0 1.0 SG A:CYS249 4.5 40.2 1.0 HG13 A:VAL312 4.6 47.0 1.0 CG2 A:VAL245 4.6 48.7 1.0 CB A:VAL312 4.6 37.9 1.0 HD11 A:LEU303 4.6 66.8 1.0 HB2 A:ARG248 4.7 37.1 1.0 HG21 A:VAL245 4.7 58.4 1.0 CD1 A:LEU317 4.7 35.6 1.0 H221 A:7SV504 4.7 45.4 1.0 HG12 A:VAL312 4.7 47.0 1.0 HE2 A:PHE316 4.7 43.7 1.0 HG A:LEU317 4.8 33.5 1.0 HD13 A:LEU317 4.8 42.7 1.0 HG22 A:VAL312 4.8 41.4 1.0 O A:VAL245 4.8 23.8 1.0 CA A:VAL245 4.8 39.8 1.0 HG23 A:VAL312 5.0 41.4 1.0 HD13 A:ILE328 5.0 58.1 1.0

Fluorine binding site 2 out of 2 in the Human Ppardelta Ligand-Binding Domain in Complexed with Specific Agonist 13


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 13 within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:56.0 occ:1.00 F30 B:7SV502 0.0 56.0 1.0 C29 B:7SV502 1.4 38.6 1.0 H311 B:7SV502 2.2 42.3 1.0 C28 B:7SV502 2.4 33.9 1.0 HG13 B:VAL245 2.4 43.5 1.0 C24 B:7SV502 2.4 33.9 1.0 HD21 B:LEU317 2.4 39.6 1.0 H281 B:7SV502 2.5 40.7 1.0 C31 B:7SV502 2.8 35.2 1.0 C23 B:7SV502 2.9 34.1 1.0 HG11 B:VAL245 3.1 43.5 1.0 CG1 B:VAL245 3.1 36.2 1.0 HG11 B:VAL312 3.1 38.0 1.0 CD2 B:LEU317 3.2 33.0 1.0 HD22 B:LEU317 3.2 39.6 1.0 HG21 B:VAL312 3.5 41.1 1.0 HG12 B:VAL245 3.6 43.5 1.0 C27 B:7SV502 3.6 30.4 1.0 HD23 B:LEU317 3.7 39.6 1.0 C25 B:7SV502 3.7 33.7 1.0 HG22 B:VAL245 3.9 47.8 1.0 HD11 B:LEU317 3.9 59.1 1.0 HG B:CYS249 4.0 44.9 1.0 C32 B:7SV502 4.0 38.7 1.0 CG1 B:VAL312 4.1 31.7 1.0 C26 B:7SV502 4.2 40.4 1.0 C22 B:7SV502 4.2 44.8 1.0 CB B:VAL245 4.3 44.2 1.0 HG21 B:VAL245 4.3 47.8 1.0 H271 B:7SV502 4.4 36.5 1.0 H321 B:7SV502 4.4 46.5 1.0 CG2 B:VAL245 4.4 39.8 1.0 CG B:LEU317 4.4 36.2 1.0 HE2 B:PHE316 4.4 55.4 1.0 CG2 B:VAL312 4.4 34.2 1.0 H251 B:7SV502 4.4 40.5 1.0 HG11 B:VAL305 4.4 45.3 1.0 HB B:VAL312 4.4 33.8 1.0 CD1 B:LEU317 4.5 49.2 1.0 HD13 B:LEU317 4.5 59.1 1.0 HG13 B:VAL312 4.6 38.0 1.0 HG12 B:VAL312 4.6 38.0 1.0 CB B:VAL312 4.6 28.2 1.0 HA B:VAL245 4.6 43.9 1.0 H221 B:7SV502 4.7 53.7 1.0 SG B:CYS249 4.7 37.4 1.0 HG B:LEU317 4.7 43.5 1.0 HD13 B:ILE328 4.8 47.2 1.0 HD11 B:LEU303 4.8 69.5 1.0 HG22 B:VAL312 4.9 41.1 1.0 HB2 B:ARG248 4.9 45.6 1.0 CA B:VAL245 5.0 36.6 1.0 HD2 B:PHE316 5.0 53.9 1.0 O B:VAL245 5.0 24.5 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