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Chlorine in PDB 4gw6: Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor

Enzymatic activity of Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor

All present enzymatic activity of Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor:
2.7.7.49; 2.7.7.7; 3.1.13.2; 3.1.26.13; 3.4.23.16;

Protein crystallography data

The structure of Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor, PDB code: 4gw6 was solved by L.Feng, M.Kvaratskhelia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.60 / 2.65
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.769, 72.769, 65.379, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 23.8

Other elements in 4gw6:

The structure of Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor also contains other interesting chemical elements:

Bromine (Br) 1 atom
Arsenic (As) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor (pdb code 4gw6). 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 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor, PDB code: 4gw6:

Chlorine binding site 1 out of 1 in 4gw6

Go back to Chlorine Binding Sites List in 4gw6
Chlorine binding site 1 out of 1 in the Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hiv-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:60.7
occ:1.00
 CL1 A:LF2303 0.0 60.7 1.0
C30 A:LF2303 1.8 58.3 1.0
C31 A:LF2303 2.7 59.6 1.0
C29 A:LF2303 2.8 58.9 1.0
CB A:TRP132 3.7 53.0 1.0
CG A:TRP132 3.9 52.0 1.0
CD2 A:LEU102 4.0 53.6 1.0
C32 A:LF2303 4.0 61.5 1.0
CD1 A:LEU102 4.1 51.5 1.0
C28 A:LF2303 4.1 58.7 1.0
CD2 A:TRP132 4.3 50.0 1.0
CA A:ALA129 4.3 51.8 1.0
O A:ALA128 4.3 54.3 1.0
CG A:LEU102 4.5 52.0 1.0
CD1 A:TRP132 4.5 53.1 1.0
C27 A:LF2303 4.6 61.8 1.0
CE3 A:TRP132 4.6 45.2 1.0
N A:ALA129 4.6 52.6 1.0
C A:ALA128 4.7 53.5 1.0
CB A:ALA129 5.0 51.2 1.0

Reference:

L.Feng, A.Sharma, A.Slaughter, N.Jena, Y.Koh, N.Shkriabai, R.C.Larue, P.A.Patel, H.Mitsuya, J.J.Kessl, A.Engelman, J.R.Fuchs, M.Kvaratskhelia. The A128T Resistance Mutation Reveals Aberrant Protein Multimerization As the Primary Mechanism of Action of Allosteric Hiv-1 Integrase Inhibitors. J.Biol.Chem. V. 288 15813 2013.
ISSN: ISSN 0021-9258
PubMed: 23615903
DOI: 10.1074/JBC.M112.443390
Page generated: Sun Jul 21 15:07:39 2024

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