Magnesium in PDB 5i3u: Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal

All present enzymatic activity of Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal:
2.7.7.49;

The structure of Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal, PDB code: 5i3u was solved by K.Das, E.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.10 / 3.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	90.240, 128.710, 131.660, 90.00, 100.84, 90.00
R / Rfree (%)	22.3 / 25.4

The binding sites of Magnesium atom in the Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal (pdb code 5i3u). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal, PDB code: 5i3u:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:79.5 occ:1.00 OD2 A:ASP443 2.2 87.1 1.0 OD1 A:ASP549 2.2 93.8 1.0 CG A:ASP443 3.2 75.7 1.0 CG A:ASP549 3.4 90.3 1.0 OD1 A:ASP443 3.5 72.4 1.0 OD2 A:ASP549 4.2 0.8 1.0 CB A:ASP549 4.2 77.1 1.0 OD2 A:ASP498 4.3 81.2 1.0 OD1 A:ASP498 4.4 86.2 1.0 O A:GLY444 4.6 80.3 1.0 CB A:ASP443 4.6 54.2 1.0 CA A:ASP549 4.6 82.4 1.0 CG A:ASP498 4.8 78.8 1.0 CE1 A:HIS539 4.8 99.0 1.0 OG A:SER553 4.9 92.0 1.0

Magnesium binding site 2 out of 2 in the Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Hiv-1 Reverse Transcriptase N-Site Complex; Catalytic Incorporation of Aztmp to A Dna Aptamer in Crystal within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:80.0 occ:1.00 OD1 C:ASP549 2.2 84.7 1.0 OD2 C:ASP443 2.2 75.5 1.0 CG C:ASP443 3.2 63.1 1.0 CG C:ASP549 3.2 80.7 1.0 OD1 C:ASP443 3.3 71.3 1.0 CB C:ASP549 4.0 78.2 1.0 OD2 C:ASP549 4.0 77.0 1.0 OD1 C:ASP498 4.4 84.7 1.0 O C:GLY444 4.4 83.0 1.0 OD2 C:ASP498 4.5 67.8 1.0 CA C:ASP549 4.5 72.5 1.0 CB C:ASP443 4.6 45.1 1.0 O C:SER553 4.7 87.0 1.0 CE1 C:HIS539 4.7 81.8 1.0 NE2 C:HIS539 4.8 84.7 1.0 CG C:ASP498 4.8 75.1 1.0 CG2 C:VAL552 5.0 77.6 1.0

K.Das, J.Balzarini, M.T.Miller, A.R.Maguire, J.J.Destefano, E.Arnold. Conformational States of Hiv-1 Reverse Transcriptase For Nucleotide Incorporation Vs Pyrophosphorolysis-Binding of Foscarnet. Acs Chem.Biol. V. 11 2158 2016.
ISSN: ESSN 1554-8937
PubMed: 27192549
DOI: 10.1021/ACSCHEMBIO.6B00187