Chlorine in PDB 3pwm: Hiv-1 Protease Mutant L76V with Darunavir

All present enzymatic activity of Hiv-1 Protease Mutant L76V with Darunavir:
3.4.23.16;

The structure of Hiv-1 Protease Mutant L76V with Darunavir, PDB code: 3pwm was solved by Y.Zhang, I.T.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.46
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.322, 86.329, 45.983, 90.00, 90.00, 90.00
R / Rfree (%)	14 / 18.9

The structure of Hiv-1 Protease Mutant L76V with Darunavir also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Hiv-1 Protease Mutant L76V with Darunavir (pdb code 3pwm). 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 L76V with Darunavir, PDB code: 3pwm:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Hiv-1 Protease Mutant L76V with Darunavir


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 L76V with Darunavir within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:15.7 occ:1.00 O A:HOH1107 3.0 25.5 0.5 O A:HOH1166 3.1 22.7 0.5 N A:THR74 3.3 11.6 1.0 ND2 A:ASN88 3.3 11.4 1.0 CA A:GLY73 3.8 11.7 1.0 CB A:ASN88 3.8 9.1 1.0 O A:HOH1270 3.9 35.3 0.5 OG1 A:THR74 3.9 14.8 1.0 CB A:THR74 3.9 13.0 1.0 CG A:ASN88 4.1 9.3 1.0 C A:GLY73 4.1 10.4 1.0 CA A:THR74 4.2 10.8 1.0 O A:HOH1058 4.4 23.4 1.0 O A:ASN88 4.7 11.0 1.0 O A:HOH1222 4.7 38.3 1.0 O A:THR74 4.7 11.8 1.0 CA A:ASN88 4.9 8.6 1.0 O A:HOH1180 5.0 39.2 0.5 C A:THR74 5.0 10.7 1.0

Chlorine binding site 2 out of 2 in the Hiv-1 Protease Mutant L76V with Darunavir


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 L76V with Darunavir within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:18.6 occ:1.00 O B:HOH1070 3.2 28.7 1.0 NE1 B:TRP106 3.3 12.2 1.0 O A:HOH1021 3.3 15.0 1.0 CZ2 B:TRP106 3.9 11.8 1.0 CE2 B:TRP106 3.9 11.9 1.0 CG2 B:THR104 4.2 17.4 1.0 O A:HOH1121 4.4 41.4 1.0 CD1 B:TRP106 4.4 11.4 1.0 CB B:THR104 4.8 13.0 1.0 O B:HOH1087 4.8 22.8 0.5

J.M.Louis, Y.Zhang, J.M.Sayer, Y.F.Wang, R.W.Harrison, I.T.Weber. The L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of Hiv-1 Protease By Reducing Internal Hydrophobic Contacts. Biochemistry V. 50 4786 2011.
ISSN: ISSN 0006-2960
PubMed: 21446746
DOI: 10.1021/BI200033Z