Fluorine in PDB 4dq5: Structural Investigation of Bacteriophage PHI6 Lysin (Wt)

The structure of Structural Investigation of Bacteriophage PHI6 Lysin (Wt), PDB code: 4dq5 was solved by M.A.Dessau, Y.Modis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.67 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.159, 68.785, 90.045, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 17.7

The binding sites of Fluorine atom in the Structural Investigation of Bacteriophage PHI6 Lysin (Wt) (pdb code 4dq5). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Structural Investigation of Bacteriophage PHI6 Lysin (Wt), PDB code: 4dq5:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Structural Investigation of Bacteriophage PHI6 Lysin (Wt)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structural Investigation of Bacteriophage PHI6 Lysin (Wt) within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:50.0 occ:0.66 F A:AES301 0.0 50.0 0.7 S A:AES301 1.5 46.7 0.7 O B:HOH605 2.4 37.8 1.0 O2S A:AES301 2.5 48.3 0.7 O1S A:AES301 2.5 39.1 0.7 C1 A:AES301 2.7 41.6 0.7 OE1 B:GLN187 2.8 42.9 1.0 CB B:GLN187 3.0 25.8 1.0 C6 A:AES301 3.0 42.4 0.7 CG B:GLN187 3.1 31.5 1.0 CD B:GLN187 3.1 43.0 1.0 O A:HOH494 3.8 31.3 1.0 O A:HOH582 3.8 31.4 1.0 C2 A:AES301 3.9 42.4 0.7 O B:HOH623 4.1 43.6 1.0 NE2 B:GLN187 4.2 42.5 1.0 CA B:GLN187 4.2 22.6 1.0 C5 A:AES301 4.4 41.2 0.7 OH A:TYR196 4.5 28.7 1.0 CE1 A:TYR196 4.5 27.4 1.0 O B:PRO183 4.7 21.7 1.0 CZ A:TYR196 4.8 25.3 1.0 N B:GLN187 4.9 21.7 1.0 CG2 B:VAL195 4.9 27.5 1.0 ND2 A:ASN118 5.0 23.7 1.0

Fluorine binding site 2 out of 2 in the Structural Investigation of Bacteriophage PHI6 Lysin (Wt)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structural Investigation of Bacteriophage PHI6 Lysin (Wt) within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:51.2 occ:0.63 F B:AES301 0.0 51.2 0.6 S B:AES301 1.5 43.3 0.6 O2S B:AES301 2.5 37.5 0.6 O A:PRO183 2.5 19.1 1.0 O1S B:AES301 2.5 39.8 0.6 C1 B:AES301 2.7 34.1 0.6 O A:HOH599 2.7 37.1 1.0 CB A:GLN187 2.9 20.6 1.0 C A:PRO183 3.1 17.3 1.0 O A:HOH515 3.3 40.6 1.0 C2 B:AES301 3.5 35.4 0.6 C6 B:AES301 3.5 30.7 0.6 N A:ALA184 3.8 17.2 1.0 CA A:ALA184 3.8 18.5 1.0 CG A:GLN187 3.8 23.5 1.0 N A:GLN187 3.9 19.0 1.0 CA A:GLN187 3.9 18.3 1.0 CA A:PRO183 4.0 18.1 1.0 OE1 A:GLN187 4.1 37.7 1.0 CB A:PRO183 4.3 21.1 1.0 O B:HOH521 4.4 36.8 1.0 CD A:GLN187 4.4 35.3 1.0 OH B:TYR196 4.4 26.7 1.0 C A:ALA184 4.5 17.0 1.0 C3 B:AES301 4.7 33.6 0.6 C5 B:AES301 4.7 34.6 0.6 O A:ALA184 4.8 17.5 1.0 CB A:ALA184 5.0 19.9 1.0

M.Dessau, D.Goldhill, R.Mcbride, R.L.Mcbride, P.E.Turner, Y.Modis. Selective Pressure Causes An Rna Virus to Trade Reproductive Fitness For Increased Structural and Thermal Stability of A Viral Enzyme. Plos Genet V. 8 03102 2012.
ISSN: ISSN 1553-7390
PubMed: 23209446
DOI: 10.1371/JOURNAL.PGEN.1003102