Fluorine in PDB 6r0h: Glycogen Phosphorylase B in Complex with 3

All present enzymatic activity of Glycogen Phosphorylase B in Complex with 3:
2.4.1.1;

The structure of Glycogen Phosphorylase B in Complex with 3, PDB code: 6r0h was solved by S.A.Tsagkarakou, M.S.Koulas, E.Kyriakis, G.A.Stravodimos, V.T.Skamnaki, D.D.Leonidas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	13.71 / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	128.287, 128.287, 116.120, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 21.3

The binding sites of Fluorine atom in the Glycogen Phosphorylase B in Complex with 3 (pdb code 6r0h). 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 Glycogen Phosphorylase B in Complex with 3, PDB code: 6r0h:

Fluorine binding site 1 out of 1 in the Glycogen Phosphorylase B in Complex with 3


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Glycogen Phosphorylase B in Complex with 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:F901 b:40.6 occ:1.00 F15 A:JN2901 0.0 40.6 1.0 C12 A:JN2901 1.4 40.5 1.0 C11 A:JN2901 2.4 35.1 1.0 C13 A:JN2901 2.4 42.7 1.0 OD1 A:ASN282 3.3 59.4 1.0 O A:TYR280 3.4 24.1 1.0 O A:ASN282 3.5 46.8 1.0 CB A:TYR280 3.6 24.7 1.0 C10 A:JN2901 3.6 37.3 1.0 C14 A:JN2901 3.7 39.8 1.0 NH2 A:ARG292 3.7 28.3 1.0 CZ A:ARG292 3.8 24.7 1.0 NH1 A:ARG292 3.8 25.2 1.0 CG A:ASN282 3.9 62.1 1.0 C A:ASN282 4.0 34.8 1.0 C A:TYR280 4.0 23.1 1.0 N A:ASN282 4.1 27.2 1.0 C9 A:JN2901 4.2 38.8 1.0 O A:HOH1188 4.3 29.7 1.0 ND2 A:ASN133 4.3 19.3 1.0 CA A:ASN282 4.4 35.4 1.0 CA A:TYR280 4.4 23.0 1.0 ND2 A:ASN282 4.4 64.1 1.0 NE A:ARG292 4.5 23.7 1.0 OE2 A:GLU88 4.6 22.4 1.0 CB A:ASN282 4.7 43.6 1.0 N A:ASP283 4.7 35.8 1.0 CG A:TYR280 4.8 25.0 1.0 N A:PRO281 4.9 23.5 1.0 C A:PRO281 4.9 23.4 1.0 O A:HOH1066 4.9 26.3 1.0 O A:PHE285 4.9 46.9 1.0

T.Fischer, S.M.Koulas, A.S.Tsagkarakou, E.Kyriakis, G.A.Stravodimos, V.T.Skamnaki, P.G.V.Liggri, S.E.Zographos, R.Riedl, D.D.Leonidas. High Consistency of Structure-Based Design and X-Ray Crystallography: Design, Synthesis, Kinetic Evaluation and Crystallographic Binding Mode Determination of Biphenyl-N-Acyl-Beta-D-Glucopyranosylamines As Glycogen Phosphorylase Inhibitors. Molecules V. 24 2019.
ISSN: ESSN 1420-3049
PubMed: 30987252
DOI: 10.3390/MOLECULES24071322