Manganese in PDB 3lp2: Hiv-1 Reverse Transcriptase with Inhibitor

All present enzymatic activity of Hiv-1 Reverse Transcriptase with Inhibitor:
2.7.7.49; 2.7.7.7; 3.1.26.4;

The structure of Hiv-1 Reverse Transcriptase with Inhibitor, PDB code: 3lp2 was solved by Y.Yan, S.K.Munshi, G.S.Prasad, H.P.Su, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	117.510, 154.780, 155.786, 90.00, 90.00, 90.00
R / Rfree (%)	24.9 / 29.6

The binding sites of Manganese atom in the Hiv-1 Reverse Transcriptase with Inhibitor (pdb code 3lp2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Hiv-1 Reverse Transcriptase with Inhibitor, PDB code: 3lp2:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Hiv-1 Reverse Transcriptase with Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Hiv-1 Reverse Transcriptase with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn602 b:0.6 occ:1.00 OD1 A:ASP443 2.4 70.6 1.0 OD2 A:ASP443 3.0 70.6 1.0 CG A:ASP443 3.1 70.0 1.0 OD1 A:ASP549 3.1 89.6 1.0 NH1 A:ARG557 3.4 93.5 1.0 MN A:MN603 3.5 92.0 1.0 O A:GLY444 3.8 71.6 1.0 OD2 A:ASP498 4.1 67.5 1.0 CG A:ASP549 4.2 89.4 1.0 NE2 A:HIS539 4.3 82.1 1.0 CZ A:ARG557 4.3 94.0 1.0 CG2 A:VAL552 4.5 89.6 1.0 CB A:ASP443 4.6 69.8 1.0 NH2 A:ARG557 4.7 94.2 1.0 CA A:ASP549 4.7 89.1 1.0 CE1 A:HIS539 4.7 82.1 1.0 C A:GLY444 4.8 71.5 1.0 CB A:ASP549 4.8 89.1 1.0 CD2 A:HIS539 4.9 81.7 1.0 CG A:ASP498 5.0 66.5 1.0

Manganese binding site 2 out of 2 in the Hiv-1 Reverse Transcriptase with Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Hiv-1 Reverse Transcriptase with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn603 b:92.0 occ:1.00 OE2 A:GLU478 2.4 69.8 1.0 OD2 A:ASP443 2.6 70.6 1.0 OD2 A:ASP498 2.8 67.5 1.0 CD A:GLU478 3.1 69.2 1.0 OD1 A:ASP498 3.1 66.9 1.0 OE1 A:GLU478 3.1 69.2 1.0 CG A:ASP498 3.3 66.5 1.0 MN A:MN602 3.5 0.6 1.0 O A:GLY444 3.6 71.6 1.0 CG A:ASP443 3.8 70.0 1.0 OD1 A:ASP443 4.3 70.6 1.0 N A:GLY444 4.3 70.4 1.0 CG A:GLU478 4.5 68.1 1.0 CB A:ASP498 4.6 66.2 1.0 C A:GLY444 4.7 71.5 1.0 C A:ASP498 4.8 66.2 1.0 O A:ASP498 4.9 66.2 1.0 CB A:ASP443 4.9 69.8 1.0 CA A:ASP443 5.0 69.8 1.0

H.P.Su, Y.Yan, G.S.Prasad, R.F.Smith, C.L.Daniels, P.D.Abeywickrema, J.C.Reid, H.M.Loughran, M.Kornienko, S.Sharma, J.A.Grobler, B.Xu, V.Sardana, T.J.Allison, P.D.Williams, P.L.Darke, D.J.Hazuda, S.Munshi. Structural Basis For the Inhibition of Rnase H Activity of Hiv-1 Reverse Transcriptase By Rnase H Active Site-Directed Inhibitors. J.Virol. V. 84 7625 2010.
ISSN: ISSN 0022-538X
PubMed: 20484498
DOI: 10.1128/JVI.00353-10