Fluorine in PDB 6d26: Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant

The structure of Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant, PDB code: 6d26 was solved by L.Wang, D.Yao, K.Deepak, H.Liu, W.Gong, H.Fan, Z.Wei, C.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.33 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.457, 61.710, 266.517, 90.00, 90.00, 90.00
R / Rfree (%)	25 / 28

The binding sites of Fluorine atom in the Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant (pdb code 6d26). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant, PDB code: 6d26:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant within 5.0Å range: probe atom residue distance (Å) B Occ A:F2401 b:88.1 occ:1.00 F23 A:FSY2401 0.0 88.1 1.0 C22 A:FSY2401 1.3 91.8 1.0 F24 A:FSY2401 2.1 92.5 1.0 F25 A:FSY2401 2.2 96.4 1.0 C21 A:FSY2401 2.3 92.9 1.0 C20 A:FSY2401 3.0 95.9 1.0 CB A:PRO2287 3.2 78.0 1.0 C16 A:FSY2401 3.3 92.6 1.0 CA A:PRO2287 3.4 77.8 1.0 CZ3 A:TRP2283 3.4 0.5 1.0 C07 A:FSY2401 3.6 60.9 1.0 C15 A:FSY2401 3.7 69.2 1.0 N A:PRO2287 4.0 80.2 1.0 CE3 A:TRP2283 4.1 0.5 1.0 CG A:PRO2287 4.2 79.5 1.0 CD A:PRO2287 4.2 80.3 1.0 C19 A:FSY2401 4.3 96.1 1.0 CH2 A:TRP2283 4.4 0.3 1.0 C17 A:FSY2401 4.5 94.0 1.0 N08 A:FSY2401 4.6 64.9 1.0 C06 A:FSY2401 4.6 61.4 1.0 C A:PRO2287 4.6 74.3 1.0 C A:LEU2286 4.7 76.3 1.0 O A:PRO2287 4.9 72.4 1.0 O A:LEU2286 4.9 75.5 1.0 C18 A:FSY2401 4.9 95.4 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant within 5.0Å range: probe atom residue distance (Å) B Occ A:F2401 b:92.5 occ:1.00 F24 A:FSY2401 0.0 92.5 1.0 C22 A:FSY2401 1.3 91.8 1.0 F23 A:FSY2401 2.1 88.1 1.0 F25 A:FSY2401 2.2 96.4 1.0 C21 A:FSY2401 2.3 92.9 1.0 C20 A:FSY2401 2.7 95.9 1.0 C16 A:FSY2401 3.6 92.6 1.0 ND1 A:HIS95 3.7 83.4 1.0 CE1 A:HIS95 3.8 84.4 1.0 C19 A:FSY2401 4.1 96.1 1.0 CB A:PRO2287 4.1 78.0 1.0 C15 A:FSY2401 4.2 69.2 1.0 CE2 A:PHE90 4.2 68.8 1.0 C17 A:FSY2401 4.7 94.0 1.0 CZ A:PHE87 4.7 92.9 1.0 CE1 A:PHE87 4.7 90.7 1.0 CA A:PRO2287 4.8 77.8 1.0 O28 A:FSY2401 4.9 77.0 1.0 C18 A:FSY2401 4.9 95.4 1.0 CD2 A:LEU91 4.9 81.1 1.0 CZ A:PHE90 5.0 73.6 1.0 CG A:HIS95 5.0 82.3 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Prostaglandin D2 Receptor CRTH2 with Fevipiprant within 5.0Å range: probe atom residue distance (Å) B Occ A:F2401 b:96.4 occ:1.00 F25 A:FSY2401 0.0 96.4 1.0 C22 A:FSY2401 1.4 91.8 1.0 F23 A:FSY2401 2.2 88.1 1.0 F24 A:FSY2401 2.2 92.5 1.0 C21 A:FSY2401 2.5 92.9 1.0 C15 A:FSY2401 2.7 69.2 1.0 C16 A:FSY2401 2.9 92.6 1.0 CZ A:PHE87 3.4 92.9 1.0 CE1 A:PHE87 3.5 90.7 1.0 C20 A:FSY2401 3.7 95.9 1.0 CA A:PRO2287 3.9 77.8 1.0 N08 A:FSY2401 4.0 64.9 1.0 CB A:PRO2287 4.0 78.0 1.0 C07 A:FSY2401 4.2 60.9 1.0 O A:PRO2287 4.2 72.4 1.0 C17 A:FSY2401 4.3 94.0 1.0 C06 A:FSY2401 4.5 61.4 1.0 C A:PRO2287 4.6 74.3 1.0 CE2 A:PHE87 4.7 93.7 1.0 C19 A:FSY2401 4.9 96.1 1.0 CD1 A:PHE87 4.9 87.9 1.0

L.Wang, D.Yao, R.N.V.K.Deepak, H.Liu, Q.Xiao, H.Fan, W.Gong, Z.Wei, C.Zhang. Structures of the Human PGD2RECEPTOR CRTH2 Reveal Novel Mechanisms For Ligand Recognition. Mol. Cell V. 72 48 2018.
ISSN: ISSN 1097-4164
PubMed: 30220562
DOI: 10.1016/J.MOLCEL.2018.08.009