Fluorine in PDB 7fou: Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08E01 From the F2X-Universal Library

The structure of Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08E01 From the F2X-Universal Library, PDB code: 7fou 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)	41.06 / 1.59
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.485, 82.111, 93.509, 90, 108.25, 90
R / Rfree (%)	20.7 / 23.9

The binding sites of Fluorine atom in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08E01 From the F2X-Universal Library (pdb code 7fou). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08E01 From the F2X-Universal Library, PDB code: 7fou:

Fluorine binding site 1 out of 1 in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P08E01 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 P08E01 From the F2X-Universal Library within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:20.0 occ:0.26 F B:VH9501 0.0 20.0 0.3 C8 B:VH9501 1.3 20.0 0.3 C7 B:VH9501 2.3 20.0 0.3 C9 B:VH9501 2.4 20.0 0.3 HA B:VAL121 2.5 52.8 1.0 HG13 B:VAL121 2.5 43.1 1.0 H B:GLN122 2.7 55.5 1.0 HG12 B:ILE126 2.9 55.3 1.0 HG13 B:ILE126 3.0 55.3 1.0 HB2 B:PHE226 3.2 39.3 1.0 CA B:VAL121 3.3 44.0 1.0 CG1 B:ILE126 3.4 46.1 1.0 CG1 B:VAL121 3.4 35.9 1.0 N B:GLN122 3.5 46.2 1.0 HG22 B:VAL121 3.5 45.8 1.0 C6 B:VH9501 3.6 20.0 0.3 C10 B:VH9501 3.6 20.0 0.3 HB2 B:LYS125 3.7 61.9 1.0 CB B:VAL121 3.8 41.7 1.0 HG12 B:VAL121 3.8 43.1 1.0 C B:VAL121 3.9 45.5 1.0 O B:GLY222 3.9 34.0 1.0 HA B:ILE126 4.0 56.6 1.0 CB B:PHE226 4.0 32.7 1.0 HB3 B:LYS125 4.0 61.9 1.0 O B:GLN122 4.1 46.1 1.0 C5 B:VH9501 4.1 20.0 0.3 HG11 B:VAL121 4.1 43.1 1.0 HA3 B:GLY222 4.1 48.3 1.0 C B:GLY222 4.1 38.1 1.0 O B:PHE120 4.1 38.5 1.0 CG2 B:VAL121 4.1 38.2 1.0 HD12 B:ILE126 4.2 48.5 1.0 N B:ILE126 4.3 45.5 1.0 CD1 B:ILE126 4.3 40.5 1.0 CG B:PHE226 4.3 34.8 1.0 HB3 B:PHE226 4.3 39.3 1.0 HA B:GLU223 4.3 46.1 1.0 HD11 B:ILE126 4.3 48.5 1.0 CB B:LYS125 4.4 51.6 1.0 H B:ILE126 4.4 54.5 1.0 CA B:ILE126 4.5 47.1 1.0 N B:VAL121 4.5 39.3 1.0 HG2 B:GLN122 4.5 67.6 1.0 CA B:GLY222 4.5 40.2 1.0 CB B:ILE126 4.5 44.4 1.0 N B:GLU223 4.6 40.3 1.0 C B:LYS125 4.6 46.1 1.0 CA B:GLN122 4.6 47.7 1.0 HA2 B:GLY222 4.7 48.3 1.0 C B:PHE120 4.7 37.4 1.0 HB B:VAL121 4.7 50.0 1.0 C B:GLN122 4.7 47.7 1.0 CD2 B:PHE226 4.7 39.1 1.0 HG21 B:VAL121 4.8 45.8 1.0 HG23 B:VAL121 4.8 45.8 1.0 CD1 B:PHE226 4.8 34.2 1.0 HD2 B:PHE226 4.8 47.0 1.0 HD2 B:LYS125 4.8 74.4 1.0 HD1 B:PHE226 4.8 41.0 1.0 HB2 B:GLN122 5.0 70.2 1.0 H B:GLU223 5.0 48.3 1.0 CA B:GLU223 5.0 38.4 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