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Atomistry » Chlorine » PDB 4gta-4h1t » 4gvm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4gta-4h1t » 4gvm » |
Chlorine in PDB 4gvm: Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric InhibitorEnzymatic activity of Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor
All present enzymatic activity of Hiv-1 Integrase Catalytic Core Domain A128T Mutant 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 A128T Mutant Complexed with Allosteric Inhibitor, PDB code: 4gvm
was solved by
L.Feng,
M.Kvaratskhelia,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4gvm:
The structure of Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor
(pdb code 4gvm). 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 A128T Mutant Complexed with Allosteric Inhibitor, PDB code: 4gvm: Chlorine binding site 1 out of 1 in 4gvmGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Hiv-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor
![]() Mono view ![]() Stereo pair view
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.
Page generated: Sun Jul 21 15:06:55 2024
ISSN: ISSN 0021-9258 PubMed: 23615903 DOI: 10.1074/JBC.M112.443390 |
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