Fluorine in PDB 7foh: Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library

The structure of Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library, PDB code: 7foh was solved by T.Barthel, J.Wollenhaupt, G.M.A.Lima, M.C.Wahl, M.S.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.27 / 1.69
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	89.397, 81.783, 93.429, 90, 108.6, 90
R / Rfree (%)	29.7 / 33.6

The binding sites of Fluorine atom in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library (pdb code 7foh). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library, PDB code: 7foh:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:20.0 occ:1.00 F B:W5U401 0.0 20.0 1.0 C8 B:W5U401 1.3 20.0 1.0 C7 B:W5U401 2.2 20.0 1.0 C9 B:W5U401 2.4 20.0 1.0 HD3 B:PRO106 2.5 72.4 1.0 O B:SER104 3.2 45.5 1.0 HG23 B:VAL103 3.2 116.9 1.0 HG21 B:ILE17 3.3 57.8 1.0 HG21 B:VAL103 3.4 116.9 1.0 C6 B:W5U401 3.4 20.0 1.0 HA B:TYR105 3.5 45.4 1.0 CD B:PRO106 3.5 60.3 1.0 HB B:VAL103 3.5 66.4 1.0 C10 B:W5U401 3.6 20.0 1.0 CG2 B:VAL103 3.6 97.4 1.0 HG23 B:ILE33 3.7 45.7 1.0 HD2 B:PRO106 3.8 72.4 1.0 C B:SER104 3.9 40.9 1.0 C5 B:W5U401 4.0 20.0 1.0 HG3 B:PRO106 4.0 77.5 1.0 CB B:VAL103 4.1 55.3 1.0 CG2 B:ILE17 4.1 48.2 1.0 HD2 B:PHE22 4.1 49.4 1.0 HE2 B:PHE22 4.2 131.1 1.0 CA B:TYR105 4.3 37.8 1.0 CD2 B:PHE22 4.3 41.2 1.0 CE2 B:PHE22 4.3 109.2 1.0 CG B:PRO106 4.3 64.6 1.0 HG22 B:ILE17 4.3 57.8 1.0 N B:TYR105 4.3 37.6 1.0 N B:PRO106 4.4 61.5 1.0 H B:SER104 4.4 53.8 1.0 HG23 B:ILE17 4.4 57.8 1.0 N B:SER104 4.5 44.8 1.0 HG22 B:VAL103 4.5 116.9 1.0 HB3 B:PRO106 4.6 92.5 1.0 HG21 B:ILE33 4.6 45.7 1.0 CG2 B:ILE33 4.6 38.1 1.0 C B:VAL103 4.7 45.9 1.0 C B:TYR105 4.7 49.6 1.0 HG12 B:ILE33 4.8 83.4 1.0 HB2 B:TYR20 4.8 96.9 1.0 CA B:SER104 4.8 38.7 1.0 HG12 B:ILE17 4.9 52.0 1.0 HG11 B:VAL103 4.9 49.9 1.0 CB B:PRO106 5.0 77.1 1.0 HB3 B:PHE22 5.0 69.5 1.0 CG B:PHE22 5.0 54.2 1.0

Fluorine binding site 2 out of 2 in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08B05 From the F2X-Universal Library within 5.0Å range: probe atom residue distance (Å) B Occ B:F402 b:20.0 occ:0.76 F B:W5U402 0.0 20.0 0.8 C8 B:W5U402 1.2 20.0 0.8 C7 B:W5U402 2.1 20.0 0.8 C9 B:W5U402 2.3 20.0 0.8 HA B:VAL121 2.4 63.4 1.0 HG12 B:VAL121 2.9 52.2 1.0 HB2 B:PHE226 3.2 49.0 1.0 H B:GLN122 3.3 125.2 0.6 H B:GLN122 3.3 122.0 0.4 C6 B:W5U402 3.4 20.0 0.8 CA B:VAL121 3.4 52.8 1.0 HG12 B:ILE126 3.4 78.9 1.0 HA3 B:GLY222 3.4 62.5 1.0 O B:GLY222 3.5 36.3 1.0 HG13 B:VAL121 3.5 52.2 1.0 CG1 B:VAL121 3.5 43.5 1.0 C10 B:W5U402 3.5 20.0 0.8 C B:GLY222 3.6 68.0 1.0 HG22 B:VAL121 3.7 57.2 1.0 HG13 B:ILE126 3.7 78.9 1.0 O B:PHE120 3.8 45.5 1.0 CB B:VAL121 3.9 50.6 1.0 HB3 B:PHE226 3.9 49.0 1.0 HA B:GLU223 3.9 42.7 1.0 CB B:PHE226 3.9 40.9 1.0 HB3 B:LYS125 3.9 111.9 1.0 CA B:GLY222 3.9 52.0 1.0 C5 B:W5U402 3.9 20.0 0.8 N B:GLN122 4.0 104.3 0.6 N B:GLN122 4.0 101.7 0.4 CG1 B:ILE126 4.1 65.7 1.0 HA2 B:GLY222 4.2 62.5 1.0 N B:GLU223 4.2 56.9 1.0 C B:VAL121 4.2 72.3 1.0 HE3 B:LYS125 4.3 115.4 1.0 HD2 B:PHE226 4.3 88.2 1.0 N B:VAL121 4.3 60.0 1.0 CG2 B:VAL121 4.3 47.7 1.0 HA B:ILE126 4.3 61.5 1.0 CG B:PHE226 4.4 61.4 1.0 HG11 B:VAL121 4.4 52.2 1.0 C B:PHE120 4.4 43.9 1.0 CD2 B:PHE226 4.5 73.5 1.0 CA B:GLU223 4.6 35.6 1.0 HB2 B:LYS125 4.6 111.9 1.0 H B:ILE126 4.6 64.6 1.0 N B:ILE126 4.7 53.8 1.0 CB B:LYS125 4.7 93.3 1.0 H B:GLU223 4.7 68.2 1.0 O B:GLN122 4.8 59.6 0.4 O B:GLN122 4.8 55.1 0.6 H B:PHE226 4.8 46.8 1.0 HD11 B:ILE129 4.8 134.3 1.0 HB B:VAL121 4.8 60.8 1.0 HD12 B:ILE126 4.8 71.4 1.0 HG23 B:VAL121 4.8 57.2 1.0 CA B:ILE126 4.9 51.2 1.0 CD1 B:ILE126 4.9 59.5 1.0 C B:LYS125 4.9 62.7 1.0 HD11 B:ILE126 5.0 71.4 1.0

T.Barthel, J.Wollenhaupt, G.M.A.Lima, M.C.Wahl, M.S.Weiss. Large-Scale Crystallographic Fragment Screening Expedites Compound Optimization and Identifies Putative Protein-Protein Interaction Sites. J.Med.Chem. V. 65 14630 2022.
ISSN: ISSN 0022-2623
PubMed: 36260741
DOI: 10.1021/ACS.JMEDCHEM.2C01165