Chlorine in PDB 2f81: Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114

All present enzymatic activity of Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114:
3.4.23.16;

The structure of Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114, PDB code: 2f81 was solved by A.Y.Kovalevsky, I.T.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.25
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.260, 85.910, 46.051, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 18.9

The structure of Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114 also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114 (pdb code 2f81). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114, PDB code: 2f81:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:18.5 occ:1.00 O A:HOH1082 3.1 36.8 1.0 OD1 A:ASN88 3.2 18.1 1.0 N A:THR74 3.3 14.7 1.0 OG1 A:THR74 3.7 19.2 1.0 CB A:ASN88 3.8 13.3 1.0 CB A:THR74 3.8 17.3 1.0 CA A:GLY73 3.8 15.7 1.0 CG A:ASN88 3.8 14.9 1.0 C A:GLY73 4.1 15.0 1.0 CA A:THR74 4.1 14.7 1.0 O A:HOH1038 4.3 25.7 1.0 O A:ASN88 4.6 14.5 1.0 OD1 A:ASP30 4.8 24.8 0.4 O A:THR74 4.8 15.4 1.0 CA A:ASN88 4.9 12.8 1.0

Chlorine binding site 2 out of 2 in the Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hiv-1 Protease Mutant L90M Complexed with Inhibitor TMC114 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:19.8 occ:1.00 NE1 B:TRP106 3.2 14.7 1.0 O A:HOH1008 3.3 16.8 1.0 O A:HOH1187 3.4 42.0 1.0 CZ2 B:TRP106 3.8 14.6 1.0 CE2 B:TRP106 3.9 14.0 1.0 CG2 B:THR104 4.3 20.6 1.0 CD1 B:TRP106 4.4 15.1 1.0 CB B:THR104 4.9 16.3 1.0 O B:HOH1089 4.9 36.8 1.0

A.Y.Kovalevsky, Y.Tie, F.Liu, P.I.Boross, Y.F.Wang, S.Leshchenko, A.K.Ghosh, R.W.Harrison, I.T.Weber. Effectiveness of Nonpeptide Clinical Inhibitor Tmc-114 on Hiv-1 Protease with Highly Drug Resistant Mutations D30N, I50V, and L90M. J.Med.Chem. V. 49 1379 2006.
ISSN: ISSN 0022-2623
PubMed: 16480273
DOI: 10.1021/JM050943C