Fluorine in PDB 5hf7: Tdg Enzyme-Substrate Complex

All present enzymatic activity of Tdg Enzyme-Substrate Complex:
3.2.2.29;

The structure of Tdg Enzyme-Substrate Complex, PDB code: 5hf7 was solved by 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)	32.51 / 1.54
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	97.030, 52.750, 81.340, 90.00, 95.18, 90.00
R / Rfree (%)	18.6 / 21.4

The binding sites of Fluorine atom in the Tdg Enzyme-Substrate Complex (pdb code 5hf7). 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 Tdg Enzyme-Substrate Complex, PDB code: 5hf7:

Fluorine binding site 1 out of 1 in the Tdg Enzyme-Substrate Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Tdg Enzyme-Substrate Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:F17 b:26.4 occ:1.00 F2' D:UF217 0.0 26.4 1.0 C2' D:UF217 1.4 17.0 1.0 C1' D:UF217 2.4 20.6 1.0 C3' D:UF217 2.4 20.3 1.0 N1 D:UF217 2.7 22.2 1.0 O4' D:UF217 3.1 18.5 1.0 ND2 A:ASN157 3.3 24.0 1.0 C4' D:UF217 3.3 20.9 1.0 C2 D:UF217 3.3 31.3 1.0 C6 D:UF217 3.4 27.3 1.0 O A:HOH436 3.4 20.2 1.0 O3' D:UF217 3.5 23.8 1.0 O2 D:UF217 3.5 38.0 1.0 O5' D:UF217 3.6 19.0 1.0 CB A:SER273 3.6 21.1 1.0 OG A:SER271 3.9 23.9 1.0 C5' D:UF217 4.1 18.6 1.0 CA A:SER273 4.1 21.2 1.0 N A:SER273 4.1 23.0 1.0 O1P D:UF217 4.1 14.4 1.0 N3 D:UF217 4.3 34.8 1.0 OG A:SER273 4.4 21.5 1.0 C5 D:UF217 4.4 26.4 1.0 P D:UF217 4.5 15.9 1.0 P D:DG18 4.6 18.6 1.0 CE1 A:TYR152 4.6 20.7 1.0 CG A:ASN157 4.6 28.7 1.0 OG A:SER272 4.7 24.7 1.0 OP2 D:DG18 4.7 18.5 1.0 O5' D:DG18 4.8 22.9 1.0 CD1 A:TYR152 4.8 24.1 1.0 C4 D:UF217 4.9 38.6 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