Fluorine in PDB 2qi0: Crystal Structure of Protease Inhibitor, Mit-1-KK80 in Complex with Wild Type Hiv-1 Protease

The structure of Crystal Structure of Protease Inhibitor, Mit-1-KK80 in Complex with Wild Type Hiv-1 Protease, PDB code: 2qi0 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)	42.37 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.975, 58.242, 61.701, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 23

The binding sites of Fluorine atom in the Crystal Structure of Protease Inhibitor, Mit-1-KK80 in Complex with Wild Type Hiv-1 Protease (pdb code 2qi0). 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 Protease Inhibitor, Mit-1-KK80 in Complex with Wild Type Hiv-1 Protease, PDB code: 2qi0:

Fluorine binding site 1 out of 1 in the Crystal Structure of Protease Inhibitor, Mit-1-KK80 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-KK80 in Complex with Wild Type Hiv-1 Protease within 5.0Å range: probe atom residue distance (Å) B Occ B:F200 b:26.0 occ:1.00 F29 B:MZ3200 0.0 26.0 1.0 C26 B:MZ3200 1.3 24.1 1.0 C27 B:MZ3200 2.4 22.7 1.0 C25 B:MZ3200 2.4 23.6 1.0 C28 B:MZ3200 2.8 25.1 1.0 CG2 A:VAL32 3.1 30.7 1.0 O A:ASP30 3.3 29.7 1.0 CB A:ASP30 3.6 28.3 1.0 C22 B:MZ3200 3.6 23.1 1.0 C24 B:MZ3200 3.6 23.8 1.0 C A:ASP30 3.8 28.2 1.0 N A:ASP30 3.8 27.3 1.0 CD1 A:ILE47 3.8 35.9 1.0 CD1 A:ILE84 3.8 37.2 1.0 CA A:ASP30 3.9 28.4 1.0 CB A:ALA28 4.1 24.5 1.0 OD2 A:ASP30 4.1 34.5 1.0 C23 B:MZ3200 4.1 25.5 1.0 CG A:ASP30 4.3 29.8 1.0 CD1 B:ILE50 4.3 34.4 1.0 CB A:VAL32 4.5 27.8 1.0 CA A:ALA28 4.6 25.1 1.0 N A:ASP29 4.7 25.9 1.0 N A:THR31 4.7 27.8 1.0 C21 B:MZ3200 4.9 22.1 1.0 C A:ALA28 4.9 25.3 1.0 CG1 A:ILE84 4.9 33.5 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