Fluorine in PDB 6oyd: X-Ray Crystal Structure of Wild Type Hiv-1 Protease in Complex with Grl-004

The structure of X-Ray Crystal Structure of Wild Type Hiv-1 Protease in Complex with Grl-004, PDB code: 6oyd was solved by H.Bulut, S.I.Hattori, H.Aoki-Ogata, H.Hayashi, M.Aoki, A.K.Ghosh, H.Mitsuya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.41 / 1.46
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	62.825, 62.825, 82.280, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 25.7

The binding sites of Fluorine atom in the X-Ray Crystal Structure of Wild Type Hiv-1 Protease in Complex with Grl-004 (pdb code 6oyd). 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 X-Ray Crystal Structure of Wild Type Hiv-1 Protease in Complex with Grl-004, PDB code: 6oyd:

Fluorine binding site 1 out of 1 in the X-Ray Crystal Structure of Wild Type Hiv-1 Protease in Complex with Grl-004


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of X-Ray Crystal Structure of Wild Type Hiv-1 Protease in Complex with Grl-004 within 5.0Å range: probe atom residue distance (Å) B Occ A:F101 b:21.4 occ:0.48 FBU A:NKA101 0.0 21.4 0.5 CBK A:NKA101 1.4 17.6 0.5 CBL A:NKA101 2.4 17.9 0.5 CBJ A:NKA101 2.4 18.6 0.5 CG A:PRO81 2.8 33.8 1.0 CB A:PRO81 3.4 29.6 1.0 CBM A:NKA101 3.7 17.4 0.5 CBI A:NKA101 3.7 17.7 0.5 CBH A:NKA101 4.2 16.6 0.5 CD A:PRO81 4.2 29.9 1.0 CG1 A:VAL82 4.3 31.6 1.0 CG2 A:VAL82 4.4 26.9 1.0 CA A:PRO81 4.6 27.6 1.0 CAD A:NKA101 4.7 15.6 0.5 C A:PRO81 4.9 29.4 1.0 N A:VAL82 4.9 23.8 1.0 CB A:VAL82 4.9 26.9 1.0 N A:PRO81 5.0 29.8 1.0 CAC A:NKA101 5.0 15.5 0.5

H.Bulut, S.I.Hattori, H.Aoki-Ogata, H.Hayashi, M.Aoki, A.K.Ghosh, H.Mitsuya. Novel Hiv-1 Protease Inhibitors, Grl-142 and Its Analogs, Markedly Adapt to the Structural Plasticity of Hiv-1 Protease and Exerts Extreme Potency with High Genetic Barrier To Be Published.