Magnesium in PDB 1vsd: Asv Integrase Core Domain with Mg(II) Cofactor and Hepes Ligand, High Mg Concentration Form

The structure of Asv Integrase Core Domain with Mg(II) Cofactor and Hepes Ligand, High Mg Concentration Form, PDB code: 1vsd was solved by G.Bujacz, M.Jaskolski, J.Alexandratos, A.Wlodawer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.050, 66.050, 81.650, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Asv Integrase Core Domain with Mg(II) Cofactor and Hepes Ligand, High Mg Concentration Form (pdb code 1vsd). 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 Asv Integrase Core Domain with Mg(II) Cofactor and Hepes Ligand, High Mg Concentration Form, PDB code: 1vsd:

Magnesium binding site 1 out of 1 in the Asv Integrase Core Domain with Mg(II) Cofactor and Hepes Ligand, High Mg Concentration Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Asv Integrase Core Domain with Mg(II) Cofactor and Hepes Ligand, High Mg Concentration Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg250 b:19.8 occ:1.00 O A:HOH262 2.0 17.0 1.0 OD2 A:ASP121 2.1 18.0 1.0 O A:HOH265 2.1 21.7 1.0 O A:HOH263 2.1 16.0 1.0 OD1 A:ASP64 2.1 14.3 1.0 O A:HOH264 2.1 20.7 1.0 CG A:ASP121 3.1 18.1 1.0 CG A:ASP64 3.1 12.1 1.0 OD2 A:ASP64 3.5 17.2 1.0 OD1 A:ASP121 3.5 17.1 1.0 O A:HOH289 4.0 17.8 1.0 O A:PHE65 4.2 16.1 1.0 CB A:ASP121 4.4 18.2 1.0 N A:PHE65 4.4 12.2 1.0 O A:HOH314 4.4 30.2 1.0 CB A:ASP64 4.5 11.1 1.0 O A:HOH379 4.7 63.2 1.0 O A:HOH371 4.8 37.9 1.0 CA A:ASP64 4.8 12.5 1.0 OZ A:OCY125 4.9 40.9 1.0 CE2 A:PHE126 5.0 14.4 1.0

G.Bujacz, M.Jaskolski, J.Alexandratos, A.Wlodawer, G.Merkel, R.A.Katz, A.M.Skalka. The Catalytic Domain of Avian Sarcoma Virus Integrase: Conformation of the Active-Site Residues in the Presence of Divalent Cations. Structure V. 4 89 1996.
ISSN: ISSN 0969-2126
PubMed: 8805516
DOI: 10.1016/S0969-2126(96)00012-3