Fluorine in PDB 6rnr: The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor

All present enzymatic activity of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor:
3.2.2.23; 4.2.99.18;

The structure of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor, PDB code: 6rnr was solved by F.Coste, S.Goffinont, B.Castaing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.91 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	91.813, 91.813, 141.617, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 19.5

The binding sites of Fluorine atom in the The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor (pdb code 6rnr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor, PDB code: 6rnr:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:54.5 occ:1.00 F01 A:KBN301 0.0 54.5 1.0 C02 A:KBN301 1.3 69.2 1.0 F04 A:KBN301 2.2 77.2 1.0 F03 A:KBN301 2.2 76.4 1.0 C05 A:KBN301 2.2 57.1 1.0 N06 A:KBN301 2.6 53.8 1.0 CG A:ARG260 3.0 37.5 1.0 CD A:ARG260 3.3 39.7 1.0 NH1 A:ARG260 3.4 35.7 1.0 N14 A:KBN301 3.6 48.5 1.0 CD1 A:LEU161 3.7 32.5 1.0 O A:ALA258 3.9 52.2 1.0 C07 A:KBN301 4.0 58.0 1.0 C7 D:DT9 4.1 36.9 1.0 NE A:ARG260 4.2 39.4 1.0 CZ A:ARG260 4.3 37.7 1.0 CB A:ARG260 4.5 38.0 1.0 CB A:LEU161 4.6 30.7 1.0 C13 A:KBN301 4.7 57.7 1.0 CG A:LEU161 4.8 35.6 1.0 C09 A:KBN301 4.9 58.5 1.0 CB A:ALA258 4.9 51.0 1.0

Fluorine binding site 2 out of 3 in the The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:76.4 occ:1.00 F03 A:KBN301 0.0 76.4 1.0 C02 A:KBN301 1.3 69.2 1.0 F04 A:KBN301 2.2 77.2 1.0 F01 A:KBN301 2.2 54.5 1.0 C05 A:KBN301 2.4 57.1 1.0 N14 A:KBN301 3.2 48.5 1.0 N06 A:KBN301 3.3 53.8 1.0 CD1 A:LEU161 3.6 32.5 1.0 CB A:LEU161 3.7 30.7 1.0 CA A:PRO158 3.9 40.4 1.0 O A:PRO158 4.1 41.2 1.0 CB A:ALA258 4.2 51.0 1.0 CB A:PRO158 4.2 42.7 1.0 CG A:LEU161 4.3 35.6 1.0 C13 A:KBN301 4.5 57.7 1.0 C A:PRO158 4.5 37.1 1.0 O A:ALA258 4.5 52.2 1.0 CG A:ARG260 4.6 37.5 1.0 C07 A:KBN301 4.6 58.0 1.0 N A:PRO158 5.0 40.0 1.0

Fluorine binding site 3 out of 3 in the The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Crystal Structure of A Complex Between the Llfpg Protein, A Thf- Dna and An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:77.2 occ:1.00 F04 A:KBN301 0.0 77.2 1.0 C02 A:KBN301 1.3 69.2 1.0 F01 A:KBN301 2.2 54.5 1.0 F03 A:KBN301 2.2 76.4 1.0 C05 A:KBN301 2.3 57.1 1.0 N14 A:KBN301 2.8 48.5 1.0 N06 A:KBN301 3.6 53.8 1.0 O A:ALA258 4.1 52.2 1.0 C7 D:DT9 4.1 36.9 1.0 C13 A:KBN301 4.2 57.7 1.0 O4 D:DT10 4.7 43.7 1.0 C07 A:KBN301 4.8 58.0 1.0 CB A:ALA258 4.8 51.0 1.0 CG A:ARG260 4.9 37.5 1.0 C09 A:KBN301 5.0 58.5 1.0

C.Rieux, S.Goffinont, F.Coste, Z.Tber, J.Cros, V.Roy, M.Guerin, V.Gaudon, S.Bourg, A.Biela, V.Aucagne, L.Agrofoglio, N.Garnier, B.Castaing. Thiopurine Derivative-Induced Fpg/Nei Dna Glycosylase Inhibition: Structural, Dynamic and Functional Insights. Int J Mol Sci V. 21 2020.
ISSN: ESSN 1422-0067
PubMed: 32192183
DOI: 10.3390/IJMS21062058