Fluorine in PDB 7flt: Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P05G04 From the F2X-Universal Library

The structure of Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P05G04 From the F2X-Universal Library, PDB code: 7flt 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)	43.30 / 1.73
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	87.839, 81.784, 93.475, 90, 107.98, 90
R / Rfree (%)	25.9 / 30.5

The binding sites of Fluorine atom in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P05G04 From the F2X-Universal Library (pdb code 7flt). 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 P05G04 From the F2X-Universal Library, PDB code: 7flt:
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 P05G04 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 P05G04 From the F2X-Universal Library within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:20.0 occ:0.88 F B:VJ0401 0.0 20.0 0.9 C6 B:VJ0401 1.2 20.0 0.9 C7 B:VJ0401 2.2 20.0 0.9 C5 B:VJ0401 2.2 20.0 0.9 HD1 B:PHE89 2.5 44.4 1.0 O B:VJ0401 2.8 20.0 0.9 HB3 B:TYR68 3.1 55.0 1.0 HB2 B:GLU83 3.1 98.7 1.0 HE1 B:PHE89 3.1 62.4 1.0 CD1 B:PHE89 3.2 37.0 1.0 CD1 B:TYR68 3.3 67.1 1.0 HD1 B:TYR68 3.3 80.5 1.0 CG B:TYR68 3.4 48.4 1.0 HG2 B:PRO5 3.5 128.5 1.0 CE1 B:PHE89 3.5 52.0 1.0 C2 B:VJ0401 3.5 20.0 0.9 HG2 B:GLU83 3.6 73.4 1.0 C4 B:VJ0401 3.6 20.0 0.9 CB B:TYR68 3.7 45.8 1.0 HB3 B:GLU83 3.7 98.7 1.0 CB B:GLU83 3.8 82.2 1.0 CE1 B:TYR68 3.8 88.3 1.0 HG21 B:ILE92 3.8 74.3 1.0 HA B:PHE89 3.9 73.8 1.0 HB2 B:TYR68 4.0 55.0 1.0 C3 B:VJ0401 4.0 20.0 0.9 CD2 B:TYR68 4.1 85.8 1.0 HG3 B:PRO5 4.1 128.5 1.0 C8 B:VJ0401 4.1 20.0 0.9 CG B:GLU83 4.2 61.1 1.0 HE1 B:TYR68 4.2 106.0 1.0 CG B:PRO5 4.2 107.1 1.0 HG13 B:ILE92 4.3 123.7 1.0 HB B:ILE92 4.3 72.7 1.0 CG B:PHE89 4.3 38.3 1.0 CZ B:TYR68 4.4 77.8 1.0 CE2 B:TYR68 4.5 63.6 1.0 HD2 B:TYR68 4.5 103.0 1.0 CG2 B:ILE92 4.5 61.9 1.0 HG22 B:ILE92 4.6 74.3 1.0 HB2 B:PHE89 4.6 43.8 1.0 C1 B:VJ0401 4.6 20.0 0.9 CA B:PHE89 4.7 61.5 1.0 CB B:PHE89 4.8 36.5 1.0 CZ B:PHE89 4.8 92.8 1.0 CB B:ILE92 4.8 60.5 1.0 HG3 B:GLU83 4.9 73.4 1.0 OE1 B:GLU83 4.9 59.0 1.0 HB2 B:PRO5 4.9 52.1 1.0 HD2 B:PRO5 4.9 52.7 1.0

Fluorine binding site 2 out of 2 in the Pandda Analysis Group Deposition -- AAR2/Rnaseh in Complex with Fragment P05G04 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 P05G04 From the F2X-Universal Library within 5.0Å range: probe atom residue distance (Å) B Occ B:F402 b:20.0 occ:0.68 F B:VJ0402 0.0 20.0 0.7 C6 B:VJ0402 1.3 20.0 0.7 C5 B:VJ0402 2.3 20.0 0.7 C7 B:VJ0402 2.3 20.0 0.7 O B:VJ0402 2.6 20.0 0.7 HB B:VAL103 2.7 88.1 1.0 HG11 B:VAL103 3.2 48.6 1.0 CB B:VAL103 3.5 73.5 1.0 HG12 B:VAL103 3.5 48.6 1.0 C4 B:VJ0402 3.6 20.0 0.7 C2 B:VJ0402 3.6 20.0 0.7 CG1 B:VAL103 3.6 40.5 1.0 HB3 B:PHE22 3.9 91.8 1.0 HG21 B:VAL103 3.9 98.2 1.0 C8 B:VJ0402 4.0 20.0 0.7 C3 B:VJ0402 4.1 20.0 0.7 CG2 B:VAL103 4.2 81.8 1.0 HB2 B:PHE22 4.2 91.8 1.0 HG23 B:VAL103 4.3 98.2 1.0 CB B:PHE22 4.3 76.5 1.0 CG B:PHE22 4.4 42.7 1.0 H B:SER104 4.4 50.1 1.0 HG13 B:VAL103 4.6 48.6 1.0 CD1 B:PHE22 4.6 52.2 1.0 HD1 B:PHE22 4.7 62.7 1.0 HA B:VAL103 4.7 38.5 1.0 CA B:VAL103 4.7 32.1 1.0 CD2 B:PHE22 4.7 69.6 1.0 C1 B:VJ0402 4.8 20.0 0.7 HD2 B:PHE22 4.9 83.5 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