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Chlorine in PDB 2bpz: Hiv-1 Protease-Inhibitor Complex

Enzymatic activity of Hiv-1 Protease-Inhibitor Complex

All present enzymatic activity of Hiv-1 Protease-Inhibitor Complex:
3.4.23.16;

Protein crystallography data

The structure of Hiv-1 Protease-Inhibitor Complex, PDB code: 2bpz was solved by S.Munshi, Z.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 58.470, 87.330, 46.660, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Hiv-1 Protease-Inhibitor Complex (pdb code 2bpz). 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-Inhibitor Complex, PDB code: 2bpz:

Chlorine binding site 1 out of 1 in 2bpz

Go back to Chlorine Binding Sites List in 2bpz
Chlorine binding site 1 out of 1 in the Hiv-1 Protease-Inhibitor Complex


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-Inhibitor Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl902

b:15.9
occ:1.00
CL1 B:3IN902 0.0 15.9 1.0
C33 B:3IN902 1.7 30.9 1.0
N6 B:3IN902 2.7 27.0 1.0
C34 B:3IN902 2.7 37.8 1.0
N5 B:3IN902 3.1 46.1 1.0
CZ A:PHE53 3.6 2.0 1.0
C37 B:3IN902 3.6 50.7 1.0
C32 B:3IN902 3.9 18.8 1.0
C26 B:3IN902 4.0 52.2 1.0
N7 B:3IN902 4.0 29.7 1.0
CE1 A:PHE53 4.2 5.2 1.0
C A:GLY48 4.2 15.1 1.0
CE2 A:PHE53 4.3 3.5 1.0
O A:GLY48 4.3 15.8 1.0
C36 B:3IN902 4.4 21.5 1.0
CA A:GLY48 4.5 13.3 1.0
N A:GLY49 4.5 16.9 1.0
O A:HOH619 4.6 25.4 1.0
O A:HOH501 4.7 8.1 1.0
N A:GLY48 4.8 12.0 1.0
CG B:PRO81 4.8 7.1 1.0
CB B:PRO81 4.8 2.4 1.0
CA A:GLY49 5.0 18.8 1.0

Reference:

S.Munshi, Z.Chen, Y.Li, D.B.Olsen, M.E.Fraley, R.W.Hungate, L.C.Kuo. Rapid X-Ray Diffraction Analysis of Hiv-1 Protease-Inhibitor Complexes: Inhibitor Exchange in Single Crystals of the Bound Enzyme. Acta Crystallogr.,Sect.D V. 54 1053 1998.
ISSN: ISSN 0907-4449
PubMed: 9757136
DOI: 10.1107/S0907444998003588
Page generated: Sat Jul 20 05:52:02 2024

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