Fluorine in PDB 4mdd: Crystal Structure of the Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12

The structure of Crystal Structure of the Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12, PDB code: 4mdd was solved by M.J.Coghlan, J.G.Luz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.80 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.543, 72.543, 229.472, 90.00, 90.00, 120.00
R / Rfree (%)	22.1 / 25.8

The binding sites of Fluorine atom in the Crystal Structure of the Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12 (pdb code 4mdd). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of the Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12, PDB code: 4mdd:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of the Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12


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 Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12 within 5.0Å range: probe atom residue distance (Å) B Occ A:F801 b:29.0 occ:1.00 F A:29M801 0.0 29.0 1.0 C11 A:29M801 1.3 28.0 1.0 C12 A:29M801 2.3 25.3 1.0 C10 A:29M801 2.4 27.3 1.0 O A:MET604 3.0 32.9 1.0 C A:MET604 3.1 34.8 1.0 N A:ALA605 3.4 31.9 1.0 CA A:ALA605 3.5 32.2 1.0 CB A:LEU608 3.6 32.6 1.0 O A:HOH948 3.6 39.6 1.0 C13 A:29M801 3.6 27.0 1.0 C9 A:29M801 3.6 26.9 1.0 CB A:MET604 3.6 34.6 1.0 CD2 A:LEU608 3.7 33.3 1.0 CA A:MET604 4.0 32.0 1.0 C8 A:29M801 4.1 27.4 1.0 O A:HOH909 4.1 49.6 1.0 CG A:LEU608 4.2 36.1 1.0 SD A:MET601 4.2 35.0 1.0 CB A:ALA605 4.4 33.3 1.0 OE1 A:GLN570 4.5 39.5 1.0 C A:ALA605 4.6 35.6 1.0 CE2 A:PHE623 4.6 36.8 1.0 CE A:MET604 4.7 38.4 1.0 O A:29M801 4.8 28.5 1.0 CA A:LEU608 4.8 33.3 1.0 CG A:MET604 4.8 38.8 1.0 CD2 A:PHE623 4.9 35.0 1.0 C14 A:29M801 4.9 25.8 1.0 O A:ALA605 4.9 35.5 1.0 N A:LEU608 4.9 33.0 1.0 CD1 A:LEU608 5.0 36.6 1.0 CE A:MET601 5.0 31.1 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12


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 Glucocorticoid Receptor Bound to A Non- Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12 within 5.0Å range: probe atom residue distance (Å) B Occ B:F801 b:30.8 occ:1.00 F B:29M801 0.0 30.8 1.0 C11 B:29M801 1.3 26.1 1.0 C10 B:29M801 2.3 25.2 1.0 C12 B:29M801 2.3 23.0 1.0 O B:MET604 2.9 38.2 1.0 C B:MET604 3.1 38.2 1.0 N B:ALA605 3.4 32.5 1.0 O B:HOH901 3.5 28.4 1.0 CB B:LEU608 3.5 25.6 1.0 CA B:ALA605 3.5 30.7 1.0 C9 B:29M801 3.6 29.8 1.0 C13 B:29M801 3.6 26.0 1.0 CD2 B:LEU608 3.6 28.7 1.0 CB B:MET604 3.7 38.0 1.0 CA B:MET604 4.0 36.3 1.0 C8 B:29M801 4.1 29.1 1.0 CG B:LEU608 4.1 29.1 1.0 O B:HOH911 4.3 37.0 1.0 OE1 B:GLN570 4.5 35.5 1.0 SD B:MET601 4.5 48.3 1.0 CB B:ALA605 4.5 30.9 1.0 CE2 B:PHE623 4.5 30.8 1.0 C B:ALA605 4.6 32.6 1.0 CE B:MET604 4.7 40.2 1.0 CA B:LEU608 4.8 26.6 1.0 CD2 B:PHE623 4.8 29.1 1.0 O B:29M801 4.8 27.2 1.0 CD1 B:LEU608 4.8 28.9 1.0 C14 B:29M801 4.9 25.0 1.0 N B:LEU608 4.9 27.5 1.0 CG B:MET604 4.9 41.2 1.0 O B:ALA605 4.9 31.6 1.0

J.G.Luz, M.J.Coghlan. Crystal Structure of the Glucocorticoid Receptor Bound to A Non-Steroidal Antagonist Reveals Repositioning and Partial Disordering of Activation Function Helix 12 To Be Published.