Fluorine in PDB 7yxo: Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment

The structure of Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment, PDB code: 7yxo was solved by A.Jimenez-Panizo, E.Estebanez-Perpina, P.Fuentes-Prior, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	90.10 / 2.99
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	180.2, 180.2, 169.18, 90, 90, 90
R / Rfree (%)	24.2 / 28

The binding sites of Fluorine atom in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment (pdb code 7yxo). 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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment, PDB code: 7yxo:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment


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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:F1001 b:37.8 occ:1.00 F1 A:DEX1001 0.0 37.8 1.0 C9 A:DEX1001 1.4 42.0 1.0 C11 A:DEX1001 2.3 45.7 1.0 C10 A:DEX1001 2.4 41.9 1.0 C8 A:DEX1001 2.4 39.6 1.0 C5 A:DEX1001 2.7 41.0 1.0 C7 A:DEX1001 2.7 38.5 1.0 C1 A:DEX1001 2.8 42.2 1.0 C14 A:DEX1001 3.0 42.2 1.0 C12 A:DEX1001 3.1 44.4 1.0 C6 A:DEX1001 3.3 37.7 1.0 C4 A:DEX1001 3.4 42.1 1.0 O2 A:DEX1001 3.5 43.2 1.0 CE1 A:PHE623 3.5 84.0 1.0 C2 A:DEX1001 3.5 41.5 1.0 C3 A:DEX1001 3.7 41.4 1.0 C13 A:DEX1001 3.7 44.1 1.0 C19 A:DEX1001 3.8 38.2 1.0 CB A:LEU563 3.9 52.8 1.0 CD1 A:PHE623 4.0 76.6 1.0 CD1 A:LEU563 4.3 51.8 1.0 C15 A:DEX1001 4.4 48.8 1.0 O1 A:DEX1001 4.6 48.0 1.0 CG A:LEU563 4.6 53.9 1.0 CZ A:PHE623 4.6 92.0 1.0 C18 A:DEX1001 4.6 38.4 1.0 O3 A:DEX1001 4.6 54.3 1.0 SD A:MET646 4.6 51.6 1.0 CE A:MET646 4.7 50.2 1.0 C17 A:DEX1001 4.8 49.1 1.0 O A:LEU563 4.8 49.9 1.0 CD2 A:LEU563 4.9 56.1 1.0 CA A:LEU563 4.9 48.0 1.0 C A:LEU563 5.0 46.0 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment


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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment within 5.0Å range: probe atom residue distance (Å) B Occ C:F1001 b:60.8 occ:1.00 F1 C:DEX1001 0.0 60.8 1.0 C9 C:DEX1001 1.4 56.5 1.0 C11 C:DEX1001 2.3 54.8 1.0 C8 C:DEX1001 2.3 58.5 1.0 C10 C:DEX1001 2.4 57.7 1.0 C5 C:DEX1001 2.8 57.6 1.0 C14 C:DEX1001 2.8 59.6 1.0 C7 C:DEX1001 2.8 60.2 1.0 C1 C:DEX1001 2.8 59.8 1.0 C12 C:DEX1001 2.9 54.8 1.0 C6 C:DEX1001 3.4 59.4 1.0 C4 C:DEX1001 3.5 64.4 1.0 C13 C:DEX1001 3.5 57.5 1.0 C2 C:DEX1001 3.5 62.3 1.0 O2 C:DEX1001 3.5 52.9 1.0 C19 C:DEX1001 3.8 57.7 1.0 CE2 C:PHE623 3.8 117.6 1.0 CE C:MET646 3.9 63.6 1.0 C3 C:DEX1001 4.0 71.1 1.0 C15 C:DEX1001 4.2 62.9 1.0 CD2 C:PHE623 4.3 113.5 1.0 O3 C:DEX1001 4.3 59.9 1.0 CB C:LEU563 4.4 33.1 1.0 C17 C:DEX1001 4.5 55.7 1.0 C18 C:DEX1001 4.6 55.0 1.0 SD C:MET646 4.6 66.2 1.0 CD1 C:LEU563 4.7 31.0 1.0 CZ C:PHE623 4.9 114.4 1.0 C16 C:DEX1001 5.0 60.0 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment


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 Wt ANCGR2-Lbd Bound to Dexamethasone and Shp Coregulator Fragment within 5.0Å range: probe atom residue distance (Å) B Occ E:F1001 b:60.6 occ:1.00 F1 E:DEX1001 0.0 60.6 1.0 C9 E:DEX1001 1.4 62.4 1.0 C11 E:DEX1001 2.3 62.8 1.0 C10 E:DEX1001 2.4 70.2 1.0 C8 E:DEX1001 2.4 58.9 1.0 C5 E:DEX1001 2.6 64.4 1.0 C7 E:DEX1001 2.8 53.0 1.0 C12 E:DEX1001 2.9 68.6 1.0 C1 E:DEX1001 2.9 77.5 1.0 C14 E:DEX1001 3.0 66.9 1.0 C4 E:DEX1001 3.2 62.2 1.0 C3 E:DEX1001 3.2 64.7 1.0 C6 E:DEX1001 3.3 57.3 1.0 C2 E:DEX1001 3.3 73.5 1.0 O2 E:DEX1001 3.5 62.4 1.0 C13 E:DEX1001 3.6 64.7 1.0 C19 E:DEX1001 3.8 67.1 1.0 O1 E:DEX1001 3.9 69.9 1.0 CB E:LEU563 4.3 66.3 1.0 CE1 E:PHE623 4.3 42.7 1.0 O3 E:DEX1001 4.4 50.9 1.0 C15 E:DEX1001 4.5 72.0 1.0 CD1 E:PHE623 4.6 46.6 1.0 C17 E:DEX1001 4.7 62.5 1.0 C18 E:DEX1001 4.7 61.8 1.0 CD1 E:LEU563 4.7 59.1 1.0 SD E:MET646 4.7 82.7 1.0 O E:LEU563 4.9 60.0 1.0

A.Jimenez-Panizo, A.Alegre-Marti, T.T.Tettey, G.Fettweis, M.Abella, R.Anton, T.A.Johnson, S.Kim, R.L.Schiltz, I.Nunez-Barrios, J.Font-Diaz, C.Caelles, A.F.Valledor, P.Perez, A.M.Rojas, J.Fernandez-Recio, D.M.Presman, G.L.Hager, P.Fuentes-Prior, E.Estebanez-Perpina. The Multivalency of the Glucocorticoid Receptor Ligand-Binding Domain Explains Its Manifold Physiological Activities. Nucleic Acids Res. 2022.
ISSN: ESSN 1362-4962
PubMed: 36464162
DOI: 10.1093/NAR/GKAC1119