Fluorine in PDB 4g90: Crystal Structure of Ribonuclease A in Complex with 5E

All present enzymatic activity of Crystal Structure of Ribonuclease A in Complex with 5E:
3.1.27.5;

The structure of Crystal Structure of Ribonuclease A in Complex with 5E, PDB code: 4g90 was solved by D.S.M.Chatzileontiadou, A.L.Kantsadi, D.D.Leonidas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	13.86 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	100.399, 32.631, 72.461, 90.00, 90.95, 90.00
R / Rfree (%)	17.5 / 23.6

The binding sites of Fluorine atom in the Crystal Structure of Ribonuclease A in Complex with 5E (pdb code 4g90). 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 Ribonuclease A in Complex with 5E, PDB code: 4g90:

Fluorine binding site 1 out of 1 in the Crystal Structure of Ribonuclease A in Complex with 5E


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 Ribonuclease A in Complex with 5E within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:34.2 occ:1.00 F5A A:0G0201 0.0 34.2 1.0 C5 A:0G0201 1.3 32.2 1.0 C4 A:0G0201 2.3 26.1 1.0 C6 A:0G0201 2.3 38.3 1.0 O4 A:0G0201 2.7 24.9 1.0 NZ A:LYS66 3.1 19.6 1.0 O A:ASP121 3.3 9.2 1.0 O A:HOH345 3.3 17.7 1.0 N3 A:0G0201 3.6 28.6 1.0 N1 A:0G0201 3.6 38.2 1.0 C A:ASP121 4.1 10.1 1.0 C2 A:0G0201 4.1 23.9 1.0 CA A:ALA122 4.1 9.0 1.0 N A:ALA122 4.4 5.5 1.0 O A:HOH354 4.4 26.2 1.0 CE A:LYS66 4.5 19.5 1.0 C7 A:0G0201 4.7 44.9 1.0 CB A:ALA122 4.7 6.1 1.0

V.Parmenopoulou, D.S.Chatzileontiadou, S.Manta, S.Bougiatioti, P.Maragozidis, D.N.Gkaragkouni, E.Kaffesaki, A.L.Kantsadi, V.T.Skamnaki, S.E.Zographos, P.Zounpoulakis, N.A.Balatsos, D.Komiotis, D.D.Leonidas. Triazole Pyrimidine Nucleosides As Inhibitors of Ribonuclease A. Synthesis, Biochemical, and Structural Evaluation. Bioorg.Med.Chem. V. 20 7184 2012.
ISSN: ISSN 0968-0896
PubMed: 23122937
DOI: 10.1016/J.BMC.2012.09.067