Magnesium in PDB 3ozg: Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate

The structure of Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate, PDB code: 3ozg was solved by M.Ho, K.Z.Hazleton, S.C.Almo, V.L.Schramm, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 1.99
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	105.095, 110.628, 173.336, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 26.4

The binding sites of Magnesium atom in the Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate (pdb code 3ozg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate, PDB code: 3ozg:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg234 b:27.3 occ:1.00 O5 A:POP233 1.9 28.7 1.0 O2 A:POP233 2.0 30.8 1.0 OD1 A:ASP204 2.0 19.9 1.0 O A:HOH289 2.0 22.2 1.0 O A:HOH290 2.1 22.5 1.0 O A:HOH269 2.5 27.1 1.0 CG A:ASP204 2.9 21.7 1.0 P1 A:POP233 3.1 28.6 1.0 P2 A:POP233 3.2 29.3 1.0 OD2 A:ASP204 3.2 21.6 1.0 O A:POP233 3.5 29.4 1.0 NH2 A:ARG210 3.8 19.4 1.0 O1 A:POP233 3.8 28.6 1.0 O A:HOH291 4.0 23.3 1.0 NH1 A:ARG210 4.1 20.7 1.0 O4 A:POP233 4.2 28.1 1.0 O6 A:POP233 4.2 27.1 1.0 O A:ASP204 4.3 23.2 1.0 O3 A:POP233 4.3 29.4 1.0 CB A:ASP204 4.3 21.1 1.0 C1' A:SSI232 4.3 25.9 1.0 N3 A:SSI232 4.4 20.5 1.0 O A:HOH287 4.4 24.4 1.0 CZ A:ARG210 4.4 23.5 1.0 N A:ASP204 4.4 20.3 1.0 CA A:ASP204 4.7 21.3 1.0 N4' A:SSI232 4.7 27.7 1.0 C A:ASP204 4.7 22.7 1.0 CB A:TYR116 5.0 27.5 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg232 b:21.9 occ:1.00 OD1 B:ASP204 2.0 28.3 1.0 O6 B:POP234 2.0 22.1 1.0 O1 B:POP234 2.1 22.9 1.0 O B:HOH283 2.1 15.3 1.0 O B:HOH284 2.2 22.5 1.0 O B:HOH256 2.3 23.8 1.0 CG B:ASP204 3.0 26.0 1.0 P2 B:POP234 3.2 22.4 1.0 P1 B:POP234 3.3 21.8 1.0 OD2 B:ASP204 3.4 27.6 1.0 O B:POP234 3.5 23.0 1.0 O5 B:POP234 4.0 23.9 1.0 O B:HOH285 4.0 24.7 1.0 NH2 B:ARG210 4.1 24.3 1.0 C1' B:SSI233 4.1 21.9 1.0 O3 B:POP234 4.2 22.5 1.0 O B:ASP204 4.3 24.2 1.0 O B:HOH252 4.3 19.8 1.0 NH1 B:ARG210 4.3 21.2 1.0 CB B:ASP204 4.4 24.4 1.0 N3 B:SSI233 4.4 18.6 1.0 O4 B:POP234 4.4 23.2 1.0 O2 B:POP234 4.4 23.6 1.0 N B:ASP204 4.5 24.4 1.0 CZ B:ARG210 4.6 22.6 1.0 N4' B:SSI233 4.7 22.2 1.0 C B:ASP204 4.7 24.7 1.0 CB B:TYR116 4.8 25.6 1.0 CA B:ASP204 4.8 24.4 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg234 b:26.1 occ:1.00 O C:HOH268 1.9 28.1 1.0 OD1 C:ASP204 1.9 22.6 1.0 O C:HOH269 2.0 19.5 1.0 O5 C:POP233 2.1 23.3 1.0 O C:HOH270 2.2 24.2 1.0 O1 C:POP233 2.3 24.9 1.0 CG C:ASP204 3.0 24.7 1.0 P2 C:POP233 3.4 25.1 1.0 OD2 C:ASP204 3.4 22.9 1.0 P1 C:POP233 3.5 25.3 1.0 O C:POP233 3.7 24.6 1.0 NH2 C:ARG210 3.9 20.1 1.0 O C:HOH265 4.0 26.2 1.0 O C:ASP204 4.1 23.5 1.0 N3 C:SSI232 4.1 23.6 1.0 O2 C:POP233 4.2 26.1 1.0 O6 C:POP233 4.2 25.6 1.0 CB C:ASP204 4.3 24.2 1.0 NH1 C:ARG210 4.3 18.5 1.0 N C:ASP204 4.3 24.8 1.0 C1' C:SSI232 4.4 22.0 1.0 O C:HOH267 4.4 21.9 1.0 O C:HOH256 4.5 28.8 1.0 O4 C:POP233 4.5 24.4 1.0 CZ C:ARG210 4.5 18.9 1.0 C C:ASP204 4.6 23.5 1.0 O3 C:POP233 4.6 26.4 1.0 CA C:ASP204 4.6 24.0 1.0 N4' C:SSI232 4.7 22.9 1.0 C2 C:SSI232 4.9 22.2 1.0 CB C:TYR116 5.0 24.9 1.0 C4 C:SSI232 5.0 23.4 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Plasmodium Falciparum Hypoxanthine-Guanine- Xanthine Phosphoribosyltransferase in Complex with S-Serme-Immh Phosphonate within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg234 b:32.6 occ:1.00 O2 D:POP233 1.8 26.2 1.0 O6 D:POP233 2.0 27.0 1.0 O D:HOH267 2.0 25.0 1.0 OD1 D:ASP204 2.2 26.8 1.0 O D:HOH266 2.3 24.4 1.0 O D:HOH263 2.4 23.1 1.0 P1 D:POP233 2.9 27.5 1.0 P2 D:POP233 3.1 28.9 1.0 O D:POP233 3.2 26.7 1.0 CG D:ASP204 3.4 28.6 1.0 O D:HOH268 3.4 21.8 1.0 O1 D:POP233 3.5 26.1 1.0 OD2 D:ASP204 3.9 29.9 1.0 O4 D:POP233 4.1 25.2 1.0 C1' D:SSI232 4.1 23.8 1.0 O5 D:POP233 4.1 25.8 1.0 O3 D:POP233 4.1 25.6 1.0 NH2 D:ARG210 4.1 26.1 1.0 NH1 D:ARG210 4.2 24.6 1.0 N3 D:SSI232 4.3 24.2 1.0 O D:ASP204 4.4 28.2 1.0 N4' D:SSI232 4.5 24.4 1.0 N D:ASP204 4.6 28.3 1.0 CB D:ASP204 4.6 27.7 1.0 O D:HOH256 4.6 24.3 1.0 CZ D:ARG210 4.6 25.5 1.0 O D:HOH265 4.7 27.3 1.0 CA D:ASP204 5.0 28.4 1.0 C D:ASP204 5.0 28.3 1.0

K.Z.Hazleton, M.C.Ho, M.B.Cassera, K.Clinch, D.R.Crump, I.Rosario, E.F.Merino, S.C.Almo, P.C.Tyler, V.L.Schramm. Acyclic Immucillin Phosphonates: Second-Generation Inhibitors of Plasmodium Falciparum Hypoxanthine- Guanine-Xanthine Phosphoribosyltransferase. Chem.Biol. V. 19 721 2012.
ISSN: ISSN 1074-5521
PubMed: 22726686
DOI: 10.1016/J.CHEMBIOL.2012.04.012