Fluorine in PDB 1d4y: Hiv-1 Protease Triple Mutant/Tipranavir Complex

All present enzymatic activity of Hiv-1 Protease Triple Mutant/Tipranavir Complex:
3.4.23.16;

The structure of Hiv-1 Protease Triple Mutant/Tipranavir Complex, PDB code: 1d4y was solved by K.D.Watenpaugh, M.N.Janakiraman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.97
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.785, 87.503, 46.458, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 21.6

The binding sites of Fluorine atom in the Hiv-1 Protease Triple Mutant/Tipranavir Complex (pdb code 1d4y). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Hiv-1 Protease Triple Mutant/Tipranavir Complex, PDB code: 1d4y:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Hiv-1 Protease Triple Mutant/Tipranavir Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Hiv-1 Protease Triple Mutant/Tipranavir Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:79.3 occ:1.00 F40 A:TPV501 0.0 79.3 1.0 C39 A:TPV501 1.4 23.8 1.0 C36 A:TPV501 2.3 30.4 1.0 F41 A:TPV501 2.4 39.2 1.0 F42 A:TPV501 2.4 48.2 1.0 C35 A:TPV501 2.7 31.3 1.0 NE B:ARG8 3.2 21.6 1.0 CZ B:ARG8 3.4 26.1 1.0 CD2 B:LEU23 3.4 20.6 1.0 C37 A:TPV501 3.5 32.9 1.0 CD B:ARG8 3.6 19.0 1.0 NH2 B:ARG8 3.8 27.4 1.0 O A:GLY27 3.8 18.3 1.0 NH1 B:ARG8 3.9 29.7 1.0 N34 A:TPV501 4.0 31.5 1.0 O A:HOH504 4.1 22.1 1.0 CD1 B:LEU23 4.4 16.5 1.0 CG B:ARG8 4.4 21.2 1.0 OD2 A:ASP29 4.4 23.2 1.0 CG B:LEU23 4.5 23.7 1.0 CG2 B:VAL82 4.6 28.5 1.0 OD1 A:ASP29 4.7 28.0 1.0 C38 A:TPV501 4.7 33.2 1.0 C33 A:TPV501 4.8 33.8 1.0 CG A:ASP29 4.9 18.0 1.0 CG1 B:VAL82 4.9 32.4 1.0 C21 A:TPV501 5.0 20.8 1.0

Fluorine binding site 2 out of 3 in the Hiv-1 Protease Triple Mutant/Tipranavir Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Hiv-1 Protease Triple Mutant/Tipranavir Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:39.2 occ:1.00 F41 A:TPV501 0.0 39.2 1.0 C39 A:TPV501 1.4 23.8 1.0 C36 A:TPV501 2.3 30.4 1.0 F40 A:TPV501 2.4 79.3 1.0 F42 A:TPV501 2.4 48.2 1.0 C37 A:TPV501 2.7 32.9 1.0 CZ B:ARG8 3.6 26.1 1.0 NH1 B:ARG8 3.6 29.7 1.0 O B:HOH173 3.6 63.7 1.0 C35 A:TPV501 3.6 31.3 1.0 NH2 B:ARG8 3.6 27.4 1.0 CG1 B:VAL82 3.9 32.4 1.0 CG2 B:VAL82 4.0 28.5 1.0 C38 A:TPV501 4.1 33.2 1.0 NE B:ARG8 4.2 21.6 1.0 CB B:VAL82 4.5 24.6 1.0 N34 A:TPV501 4.7 31.5 1.0 O A:HOH590 4.8 90.3 1.0 O B:HOH172 4.8 63.6 1.0 CD B:ARG8 4.8 19.0 1.0 C33 A:TPV501 4.9 33.8 1.0

Fluorine binding site 3 out of 3 in the Hiv-1 Protease Triple Mutant/Tipranavir Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Hiv-1 Protease Triple Mutant/Tipranavir Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:48.2 occ:1.00 F42 A:TPV501 0.0 48.2 1.0 C39 A:TPV501 1.4 23.8 1.0 C36 A:TPV501 2.3 30.4 1.0 F40 A:TPV501 2.4 79.3 1.0 F41 A:TPV501 2.4 39.2 1.0 C22 A:TPV501 3.0 26.9 1.0 C35 A:TPV501 3.1 31.3 1.0 CG2 B:VAL82 3.2 28.5 1.0 C37 A:TPV501 3.3 32.9 1.0 C21 A:TPV501 3.4 20.8 1.0 CD2 B:LEU23 3.7 20.6 1.0 N34 A:TPV501 4.2 31.5 1.0 CB B:VAL82 4.3 24.6 1.0 CG1 B:VAL82 4.4 32.4 1.0 O A:GLY27 4.4 18.3 1.0 C38 A:TPV501 4.5 33.2 1.0 CD1 B:ILE84 4.7 38.0 1.0 C33 A:TPV501 4.8 33.8 1.0 C20 A:TPV501 4.9 20.6 1.0

S.Thaisrivongs, H.I.Skulnick, S.R.Turner, J.W.Strohbach, R.A.Tommasi, P.D.Johnson, P.A.Aristoff, T.M.Judge, R.B.Gammill, J.K.Morris, K.R.Romines, R.A.Chrusciel, R.R.Hinshaw, K.T.Chong, W.G.Tarpley, S.M.Poppe, D.E.Slade, J.C.Lynn, M.M.Horng, P.K.Tomich, E.P.Seest, L.A.Dolak, W.J.Howe, G.M.Howard, K.D.Watenpaugh. Structure-Based Design of Hiv Protease Inhibitors: Sulfonamide-Containing 5,6-Dihydro-4-Hydroxy-2-Pyrones As Non-Peptidic Inhibitors. J.Med.Chem. V. 39 4349 1996.
ISSN: ISSN 0022-2623
PubMed: 8893827
DOI: 10.1021/JM960541S