Magnesium in PDB 7otz: Hiv-1 Reverse Transcriptase Complex with Dna and Inhibitor Rmc-259

All present enzymatic activity of Hiv-1 Reverse Transcriptase Complex with Dna and Inhibitor Rmc-259:
2.7.7.49; 2.7.7.7; 3.1.13.2; 3.1.26.13;

The structure of Hiv-1 Reverse Transcriptase Complex with Dna and Inhibitor Rmc-259, PDB code: 7otz was solved by S.E.Martinez, A.K.Singh, W.Gu, K.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	96.19 / 3.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	89.748, 133.13, 140.368, 90, 97.59, 90
R / Rfree (%)	21 / 25.7

The binding sites of Magnesium atom in the Hiv-1 Reverse Transcriptase Complex with Dna and Inhibitor Rmc-259 (pdb code 7otz). 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 Hiv-1 Reverse Transcriptase Complex with Dna and Inhibitor Rmc-259, PDB code: 7otz:

Magnesium binding site 1 out of 1 in the Hiv-1 Reverse Transcriptase Complex with Dna and Inhibitor Rmc-259


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hiv-1 Reverse Transcriptase Complex with Dna and Inhibitor Rmc-259 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:156.5 occ:1.00 OD1 A:ASP185 2.1 148.5 1.0 O22 A:1IO602 2.1 167.2 1.0 O21 A:1IO602 2.4 168.1 1.0 CG A:ASP185 2.6 131.0 1.0 C20 A:1IO602 2.6 173.2 1.0 OD2 A:ASP185 2.7 124.5 1.0 OD2 A:ASP110 2.8 165.6 1.0 OD1 A:ASP110 3.4 177.5 1.0 CG A:ASP110 3.5 178.2 1.0 CB A:ASP185 3.7 123.5 1.0 C3' P:DDG822 3.8 138.1 1.0 C2' P:DDG822 4.1 136.7 1.0 C14 A:1IO602 4.1 183.0 1.0 O A:VAL111 4.1 147.6 1.0 O13 A:1IO602 4.8 182.5 1.0 CB A:ASP110 4.9 169.4 1.0 CA A:ASP185 5.0 122.4 1.0

W.Gu, S.E.Martinez, A.K.Singh, H.Nguyen, J.Rozenski, D.Schols, P.Herdewijn, K.Das, S.De Jonghe. Exploring the Dntp -Binding Site of Hiv-1 Reverse Transcriptase For Inhibitor Design Eur.J.Med.Chem. V. 225 2021.
ISSN: ISSN 0223-5234
DOI: 10.1016/J.EJMECH.2021.113785