Fluorine in PDB 2o4n: Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir

The structure of Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir, PDB code: 2o4n was solved by L.W.Kang, A.A.Armstrong, S.Muzammil, A.Jakalian, P.R.Bonneau, V.Schmelmer, E.Freire, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.60 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.076, 86.487, 46.439, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 22.7

The binding sites of Fluorine atom in the Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir (pdb code 2o4n). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir, PDB code: 2o4n:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir


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 Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir within 5.0Å range: probe atom residue distance (Å) B Occ A:F300 b:25.4 occ:1.00 F40 A:TPV300 0.0 25.4 1.0 C39 A:TPV300 1.3 24.0 1.0 F42 A:TPV300 2.1 24.9 1.0 F41 A:TPV300 2.2 24.7 1.0 C36 A:TPV300 2.4 21.1 1.0 C35 A:TPV300 2.9 22.8 1.0 NE B:ARG8 3.2 24.0 1.0 CZ B:ARG8 3.3 26.7 1.0 CD B:ARG8 3.5 21.0 1.0 C37 A:TPV300 3.6 23.8 1.0 CD1 B:LEU82 3.6 24.3 1.0 NH1 B:ARG8 3.7 25.0 1.0 CD2 B:LEU23 3.7 21.1 1.0 NH2 B:ARG8 3.8 24.0 1.0 O A:GLY27 3.9 18.4 1.0 O A:HOH321 4.0 25.0 1.0 CD1 B:LEU23 4.2 16.2 1.0 OD1 A:ASP29 4.2 20.6 1.0 N34 A:TPV300 4.3 20.8 1.0 CD2 B:LEU82 4.3 23.3 1.0 CG B:ARG8 4.3 20.4 1.0 CG B:LEU82 4.6 22.5 1.0 CG B:LEU23 4.6 19.1 1.0 C38 A:TPV300 4.8 23.7 1.0 CG A:ASP29 4.9 21.3 1.0 OD2 A:ASP29 4.9 22.5 1.0 C22 A:TPV300 5.0 17.3 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir within 5.0Å range: probe atom residue distance (Å) B Occ A:F300 b:24.7 occ:1.00 F41 A:TPV300 0.0 24.7 1.0 C39 A:TPV300 1.3 24.0 1.0 F42 A:TPV300 2.1 24.9 1.0 F40 A:TPV300 2.2 25.4 1.0 C36 A:TPV300 2.3 21.1 1.0 C37 A:TPV300 2.7 23.8 1.0 CZ B:ARG8 3.4 26.7 1.0 O B:HOH373 3.4 39.0 1.0 NH1 B:ARG8 3.4 25.0 1.0 CD1 B:LEU82 3.5 24.3 1.0 NH2 B:ARG8 3.5 24.0 1.0 C35 A:TPV300 3.6 22.8 1.0 CD2 B:LEU82 4.0 23.3 1.0 O B:HOH350 4.0 36.0 1.0 NE B:ARG8 4.1 24.0 1.0 C38 A:TPV300 4.1 23.7 1.0 CG B:LEU82 4.3 22.5 1.0 O B:HOH376 4.3 36.6 1.0 N34 A:TPV300 4.7 20.8 1.0 CD B:ARG8 4.7 21.0 1.0 CB B:PRO81 4.8 23.8 1.0 C33 A:TPV300 5.0 21.9 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Hiv-1 Protease (Trm Mutant) in Complex with Tipranavir within 5.0Å range: probe atom residue distance (Å) B Occ A:F300 b:24.9 occ:1.00 F42 A:TPV300 0.0 24.9 1.0 C39 A:TPV300 1.3 24.0 1.0 F41 A:TPV300 2.1 24.7 1.0 F40 A:TPV300 2.1 25.4 1.0 C36 A:TPV300 2.3 21.1 1.0 C35 A:TPV300 3.0 22.8 1.0 CD2 B:LEU82 3.1 23.3 1.0 C37 A:TPV300 3.2 23.8 1.0 C22 A:TPV300 3.4 17.3 1.0 CD1 B:LEU82 3.7 24.3 1.0 C21 A:TPV300 3.7 19.5 1.0 CD2 B:LEU23 3.9 21.1 1.0 CG B:LEU82 4.0 22.5 1.0 N34 A:TPV300 4.3 20.8 1.0 O A:GLY27 4.3 18.4 1.0 C38 A:TPV300 4.4 23.7 1.0 CG B:PRO81 4.6 23.0 1.0 CB B:PRO81 4.8 23.8 1.0 C33 A:TPV300 4.8 21.9 1.0 O B:HOH373 4.9 39.0 1.0 C20 A:TPV300 4.9 19.2 1.0 CZ B:ARG8 4.9 26.7 1.0

S.Muzammil, A.A.Armstrong, L.W.Kang, A.Jakalian, P.R.Bonneau, V.Schmelmer, L.M.Amzel, E.Freire. Unique Thermodynamic Response of Tipranavir to Human Immunodeficiency Virus Type 1 Protease Drug Resistance Mutations. J.Virol. V. 81 5144 2007.
ISSN: ISSN 0022-538X
PubMed: 17360759
DOI: 10.1128/JVI.02706-06