Magnesium in PDB 5oi3: Dissociation of Biochemical and Antiretroviral Activities of Integrase-Ledgf Allosteric Inhibitors Revealed By Resistance of A125 Polymorphic Hiv-1

The structure of Dissociation of Biochemical and Antiretroviral Activities of Integrase-Ledgf Allosteric Inhibitors Revealed By Resistance of A125 Polymorphic Hiv-1, PDB code: 5oi3 was solved by M.Ruff, R.Benarous, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.18 / 2.30
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.363, 72.363, 65.819, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 27.2

The structure of Dissociation of Biochemical and Antiretroviral Activities of Integrase-Ledgf Allosteric Inhibitors Revealed By Resistance of A125 Polymorphic Hiv-1 also contains other interesting chemical elements:

Arsenic

(As)

2 atoms

The binding sites of Magnesium atom in the Dissociation of Biochemical and Antiretroviral Activities of Integrase-Ledgf Allosteric Inhibitors Revealed By Resistance of A125 Polymorphic Hiv-1 (pdb code 5oi3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Dissociation of Biochemical and Antiretroviral Activities of Integrase-Ledgf Allosteric Inhibitors Revealed By Resistance of A125 Polymorphic Hiv-1, PDB code: 5oi3:

Magnesium binding site 1 out of 1 in the Dissociation of Biochemical and Antiretroviral Activities of Integrase-Ledgf Allosteric Inhibitors Revealed By Resistance of A125 Polymorphic Hiv-1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dissociation of Biochemical and Antiretroviral Activities of Integrase-Ledgf Allosteric Inhibitors Revealed By Resistance of A125 Polymorphic Hiv-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:55.9 occ:1.00 O A:HOH413 2.7 49.6 1.0 O A:HOH409 2.8 58.8 1.0 N A:CAS65 3.1 37.2 1.0 ND2 A:ASN120 3.1 34.5 1.0 CA A:ASP64 3.6 38.9 1.0 CB A:ASP64 3.6 39.3 1.0 OD1 A:ASP64 3.7 42.9 1.0 O A:CAS65 3.7 44.2 1.0 C A:ASP64 3.9 37.6 1.0 CB A:ASN117 4.0 34.7 1.0 AS A:CAS65 4.1 46.4 1.0 CA A:CAS65 4.1 41.6 1.0 CG A:ASP64 4.1 43.1 1.0 CG A:ASN120 4.2 38.0 1.0 CB A:CAS65 4.2 43.0 1.0 OD1 A:ASN120 4.3 38.3 1.0 C A:CAS65 4.3 45.2 1.0 OG1 A:THR115 4.5 34.0 1.0 OE2 A:GLU92 4.6 64.5 1.0 CE2 A:CAS65 4.6 41.4 1.0 N A:ASN117 4.7 34.5 1.0 ND2 A:ASN117 4.8 36.8 1.0 N A:ASP64 4.9 35.1 1.0 O A:LEU63 5.0 33.5 1.0 CG A:ASN117 5.0 37.1 1.0 CA A:ASN117 5.0 32.6 1.0

D.Bonnard, E.Le Rouzic, S.Eiler, C.Amadori, I.Orlov, J.M.Bruneau, J.Brias, J.Barbion, F.Chevreuil, D.Spehner, S.Chasset, B.Ledoussal, F.Moreau, A.Saib, B.P.Klaholz, S.Emiliani, M.Ruff, A.Zamborlini, R.Benarous. Structure-Function Analyses Unravel Distinct Effects of Allosteric Inhibitors of Hiv-1 Integrase on Viral Maturation and Integration. J. Biol. Chem. V. 293 6172 2018.
ISSN: ESSN 1083-351X
PubMed: 29507092
DOI: 10.1074/JBC.M117.816793