Fluorine in PDB 2qhy: Crystal Structure of Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease

The structure of Crystal Structure of Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease, PDB code: 2qhy was solved by C.A.Schiffer, M.N.L.Nalam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.18 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.670, 57.981, 61.541, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 19.7

The binding sites of Fluorine atom in the Crystal Structure of Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease (pdb code 2qhy). 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 Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease, PDB code: 2qhy:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease


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 Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease within 5.0Å range: probe atom residue distance (Å) B Occ A:F200 b:23.3 occ:1.00 F1 A:MZ1200 0.0 23.3 1.0 C7 A:MZ1200 1.4 23.7 1.0 C2 A:MZ1200 2.3 22.7 1.0 C6 A:MZ1200 2.4 22.0 1.0 F2 A:MZ1200 2.7 24.0 1.0 O B:HOH542 3.1 31.9 1.0 O B:HOH512 3.3 16.7 1.0 CB B:ILE47 3.4 21.4 1.0 O B:GLY48 3.4 22.3 1.0 C3 A:MZ1200 3.6 22.7 1.0 N B:GLY48 3.7 21.7 1.0 C5 A:MZ1200 3.7 22.8 1.0 O B:HOH511 3.9 14.5 1.0 CG2 B:ILE47 3.9 21.0 1.0 CA B:ILE47 4.1 21.4 1.0 C4 A:MZ1200 4.1 23.1 1.0 O B:HOH594 4.2 33.7 1.0 C B:ILE47 4.2 21.7 1.0 C B:GLY48 4.3 22.6 1.0 O B:HOH581 4.3 36.1 1.0 CG1 B:ILE47 4.4 21.6 1.0 CD1 B:ILE47 4.5 22.1 1.0 CA B:GLY48 4.6 22.2 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease


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 Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease within 5.0Å range: probe atom residue distance (Å) B Occ A:F200 b:23.6 occ:1.00 F3 A:MZ1200 0.0 23.6 1.0 C4 A:MZ1200 1.3 23.1 1.0 C3 A:MZ1200 2.3 22.7 1.0 C5 A:MZ1200 2.4 22.8 1.0 O10 A:MZ1200 2.9 24.0 1.0 S8 A:MZ1200 3.0 23.4 1.0 CB B:ALA28 3.0 17.9 1.0 C16 A:MZ1200 3.3 23.4 1.0 CG2 B:ILE84 3.5 18.8 1.0 CD1 B:ILE84 3.5 18.4 1.0 N11 A:MZ1200 3.5 25.1 1.0 C2 A:MZ1200 3.6 22.7 1.0 C6 A:MZ1200 3.6 22.0 1.0 CA B:ALA28 3.8 17.8 1.0 OD1 B:ASP25 4.1 19.8 1.0 C7 A:MZ1200 4.1 23.7 1.0 O B:ASP30 4.2 18.6 1.0 CB B:ILE84 4.2 18.5 1.0 CG2 B:VAL32 4.3 20.5 1.0 CG1 B:ILE84 4.3 18.5 1.0 O9 A:MZ1200 4.3 23.7 1.0 C12 A:MZ1200 4.4 25.2 1.0 C17 A:MZ1200 4.6 23.8 1.0 CD1 A:ILE50 4.7 22.3 1.0 F2 A:MZ1200 4.7 24.0 1.0 N B:ALA28 4.8 18.0 1.0 O B:HOH511 4.8 14.5 1.0 C32 A:MZ1200 4.8 23.9 1.0 CG B:ASP25 4.9 19.4 1.0 C B:ALA28 4.9 18.1 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease


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 Protease Inhibitor, Mit-1-AC86 in Complex with Wild Type Hiv-1 Protease within 5.0Å range: probe atom residue distance (Å) B Occ A:F200 b:24.0 occ:1.00 F2 A:MZ1200 0.0 24.0 1.0 C2 A:MZ1200 1.4 22.7 1.0 C7 A:MZ1200 2.4 23.7 1.0 C3 A:MZ1200 2.4 22.7 1.0 F1 A:MZ1200 2.7 23.3 1.0 O B:HOH542 2.9 31.9 1.0 CB B:ASP30 3.4 19.0 1.0 OD2 B:ASP30 3.4 26.2 1.0 C6 A:MZ1200 3.7 22.0 1.0 C4 A:MZ1200 3.7 23.1 1.0 CG B:ASP30 3.8 21.7 1.0 O B:HOH511 3.8 14.5 1.0 N B:ASP30 3.9 18.6 1.0 CG2 B:ILE47 4.1 21.0 1.0 CA B:ASP30 4.1 19.0 1.0 CD1 B:LEU76 4.2 17.8 1.0 C5 A:MZ1200 4.2 22.8 1.0 O B:ASP30 4.2 18.6 1.0 CD1 B:ILE47 4.3 22.1 1.0 CB B:ILE47 4.3 21.4 1.0 CG2 B:VAL32 4.4 20.5 1.0 C B:ASP30 4.4 18.9 1.0 F3 A:MZ1200 4.7 23.6 1.0 N B:ASP29 4.8 18.3 1.0 OD1 B:ASP30 4.9 21.9 1.0 CG1 B:ILE47 4.9 21.6 1.0 CB B:ASP29 5.0 18.5 1.0 C B:ASP29 5.0 18.6 1.0

M.D.Altman, A.Ali, G.S.Reddy, M.N.Nalam, S.G.Anjum, H.Cao, S.Chellappan, V.Kairys, M.X.Fernandes, M.K.Gilson, C.A.Schiffer, T.M.Rana, B.Tidor. Hiv-1 Protease Inhibitors From Inverse Design in the Substrate Envelope Exhibit Subnanomolar Binding to Drug-Resistant Variants. J.Am.Chem.Soc. V. 130 6099 2008.
ISSN: ISSN 0002-7863
PubMed: 18412349
DOI: 10.1021/JA076558P