Fluorine in PDB 5jxy: Enzyme-Substrate Complex of Tdg Catalytic Domain Bound to A G/U Analog

All present enzymatic activity of Enzyme-Substrate Complex of Tdg Catalytic Domain Bound to A G/U Analog:
3.2.2.29;

The structure of Enzyme-Substrate Complex of Tdg Catalytic Domain Bound to A G/U Analog, PDB code: 5jxy was solved by L.S.Pidugu, E.Pozharski, S.S.Malik, A.C.Drohat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.70 / 1.71
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.450, 53.270, 82.540, 90.00, 95.63, 90.00
R / Rfree (%)	19.8 / 23.1

The binding sites of Fluorine atom in the Enzyme-Substrate Complex of Tdg Catalytic Domain Bound to A G/U Analog (pdb code 5jxy). 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 Enzyme-Substrate Complex of Tdg Catalytic Domain Bound to A G/U Analog, PDB code: 5jxy:

Fluorine binding site 1 out of 1 in the Enzyme-Substrate Complex of Tdg Catalytic Domain Bound to A G/U Analog


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Enzyme-Substrate Complex of Tdg Catalytic Domain Bound to A G/U Analog within 5.0Å range: probe atom residue distance (Å) B Occ D:F17 b:19.3 occ:1.00 F2' D:UF217 0.0 19.3 1.0 C2' D:UF217 1.4 17.6 1.0 C3' D:UF217 2.4 16.2 1.0 C1' D:UF217 2.4 16.1 1.0 N1 D:UF217 2.7 17.3 1.0 O4' D:UF217 3.1 17.1 1.0 ND2 A:ASN157 3.1 13.4 1.0 C6 D:UF217 3.3 16.8 1.0 C4' D:UF217 3.3 17.7 1.0 C2 D:UF217 3.4 19.4 1.0 O A:HOH431 3.4 20.2 1.0 O3' D:UF217 3.4 20.3 1.0 O5' D:UF217 3.6 18.8 1.0 O2 D:UF217 3.6 19.9 1.0 CB A:SER273 3.7 17.4 1.0 OG A:SER271 4.0 17.5 1.0 N A:SER273 4.1 16.4 1.0 CA A:SER273 4.1 16.2 1.0 C5' D:UF217 4.1 19.2 1.0 O2P D:UF217 4.2 18.4 1.0 C5 D:UF217 4.3 19.7 1.0 CE1 A:TYR152 4.3 17.1 1.0 CG A:ASN157 4.4 20.2 1.0 N3 D:UF217 4.4 20.5 1.0 OG A:SER273 4.5 17.8 1.0 CD1 A:TYR152 4.5 16.7 1.0 P D:UF217 4.6 19.4 1.0 P D:DG18 4.7 20.9 1.0 OG A:SER272 4.7 17.9 1.0 OD1 A:ASN157 4.8 17.5 1.0 C4 D:UF217 4.8 21.2 1.0 OP2 D:DG18 4.9 19.3 1.0 O5' D:DG18 4.9 20.3 1.0

C.T.Coey, S.S.Malik, L.S.Pidugu, K.M.Varney, E.Pozharski, A.C.Drohat. Structural Basis of Damage Recognition By Thymine Dna Glycosylase: Key Roles For N-Terminal Residues. Nucleic Acids Res. V. 44 10248 2016.
ISSN: ESSN 1362-4962
PubMed: 27580719
DOI: 10.1093/NAR/GKW768