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Chlorine in PDB 3pwr: Hiv-1 Protease Mutant L76V Complexed with Saquinavir

Enzymatic activity of Hiv-1 Protease Mutant L76V Complexed with Saquinavir

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

Protein crystallography data

The structure of Hiv-1 Protease Mutant L76V Complexed with Saquinavir, PDB code: 3pwr 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 / 1.45
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 58.840, 86.170, 46.240, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 19.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Hiv-1 Protease Mutant L76V Complexed with Saquinavir (pdb code 3pwr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Hiv-1 Protease Mutant L76V Complexed with Saquinavir, PDB code: 3pwr:

Chlorine binding site 1 out of 1 in 3pwr

Go back to Chlorine Binding Sites List in 3pwr
Chlorine binding site 1 out of 1 in the Hiv-1 Protease Mutant L76V Complexed with Saquinavir


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 Complexed with Saquinavir within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:18.8
occ:1.00
N A:THR74 3.3 16.6 1.0
ND2 A:ASN88 3.3 15.2 1.0
C3 A:GOL405 3.8 43.5 0.5
CB A:ASN88 3.8 14.2 1.0
CA A:GLY73 3.8 16.0 1.0
CB A:THR74 3.9 15.8 1.0
OG1 A:THR74 3.9 19.3 1.0
C A:GLY73 4.0 14.2 1.0
CG A:ASN88 4.1 15.1 1.0
CA A:THR74 4.2 15.1 1.0
O A:HOH520 4.4 29.0 1.0
O3 A:GOL405 4.4 48.1 0.5
C1 A:GOL405 4.5 39.4 0.5
O A:HOH584 4.6 58.4 1.0
O A:THR74 4.7 15.7 1.0
O A:ASN88 4.7 15.4 1.0
C2 A:GOL405 4.7 41.7 0.5
CA A:ASN88 4.9 13.9 1.0
C A:THR74 4.9 14.7 1.0
O1 A:GOL405 5.0 31.2 0.5

Reference:

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
Page generated: Sun Jul 21 02:37:51 2024

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