Fluorine in PDB 8t1u: Crystal Structure of the DRM2-Cta Dna Complex

All present enzymatic activity of Crystal Structure of the DRM2-Cta Dna Complex:
2.1.1.37;

The structure of Crystal Structure of the DRM2-Cta Dna Complex, PDB code: 8t1u was solved by J.Chen, J.Lu, J.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.41 / 2.91
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	54.469, 232.853, 118.497, 90, 90, 90
R / Rfree (%)	20.6 / 25.3

The binding sites of Fluorine atom in the Crystal Structure of the DRM2-Cta Dna Complex (pdb code 8t1u). 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 Crystal Structure of the DRM2-Cta Dna Complex, PDB code: 8t1u:

Fluorine binding site 1 out of 1 in the Crystal Structure of the DRM2-Cta Dna Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the DRM2-Cta Dna Complex within 5.0Å range: probe atom residue distance (Å) B Occ G:F10 b:46.0 occ:1.00 F G:C4910 0.0 46.0 1.0 C5 G:C4910 1.4 40.8 1.0 C4 G:C4910 2.3 40.6 1.0 SG A:CYS587 2.3 30.8 1.0 CB A:CYS587 2.4 27.3 1.0 C6 G:C4910 2.4 26.3 1.0 CM5 G:C4910 2.4 26.2 1.0 N A:CYS587 2.6 34.0 1.0 N4 G:C4910 2.7 25.5 1.0 CA A:CYS587 3.0 31.4 1.0 N3 G:C4910 3.4 29.5 1.0 N1 G:C4910 3.5 21.7 1.0 OD1 A:ASN313 3.5 14.4 1.0 O A:SER585 3.6 29.0 1.0 C A:PRO586 3.6 31.3 1.0 C2 G:C4910 3.9 26.2 1.0 CA A:PRO586 4.1 23.7 1.0 C A:CYS587 4.2 29.4 1.0 CG A:ASN313 4.3 14.3 1.0 CG1 A:VAL314 4.5 22.1 1.0 C A:SER585 4.6 23.2 1.0 O A:PRO586 4.6 38.4 1.0 C1' G:C4910 4.7 29.0 1.0 ND2 A:ASN313 4.8 16.3 1.0 OD1 A:ASN480 4.8 39.1 1.0 N A:VAL314 4.8 17.6 1.0 N A:PRO586 4.9 22.4 1.0 CA A:ASN313 4.9 19.7 1.0 N A:ASN588 4.9 35.7 1.0 O A:CYS587 4.9 26.7 1.0 OE2 A:GLU312 5.0 25.6 1.0

J.Chen, J.Lu, J.Liu, J.Fang, X.Zhong, J.Song. Dna Conformational Dynamics in the Context-Dependent Non-Cg Chh Methylation By Plant Methyltransferase DRM2. J.Biol.Chem. 05433 2023.
ISSN: ESSN 1083-351X
PubMed: 37926286
DOI: 10.1016/J.JBC.2023.105433