Magnesium in PDB 3koa: M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp

All present enzymatic activity of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp:
2.7.7.48;

The structure of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp, PDB code: 3koa was solved by C.Ferrer-Orta, N.Verdaguer, R.Perez-Luque, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.89 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.371, 95.371, 100.878, 90.00, 90.00, 120.00
R / Rfree (%)	22.3 / 29

The binding sites of Magnesium atom in the M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp (pdb code 3koa). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp, PDB code: 3koa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1030 b:63.0 occ:1.00 OD2 A:ASP238 2.5 53.4 1.0 O A:HOH484 2.8 32.2 1.0 OD1 A:ASP240 3.1 52.3 1.0 O A:THR384 3.4 42.1 1.0 OD1 A:ASP339 3.5 41.2 1.0 CG A:ASP238 3.6 51.9 1.0 OD1 A:ASP238 4.0 54.0 1.0 CG A:ASP240 4.3 51.1 1.0 C A:THR384 4.3 40.7 1.0 CB A:ALA367 4.3 55.3 1.0 CG A:ASP339 4.4 38.0 1.0 O A:ILE340 4.6 40.9 1.0 OD2 A:ASP240 4.7 55.1 1.0 OD2 A:ASP339 4.7 39.2 1.0 CG2 A:THR384 4.7 42.8 1.0 O A:VAL239 4.8 47.7 1.0 CB A:THR384 4.8 42.7 1.0 CB A:ASP238 4.9 50.4 1.0

Magnesium binding site 2 out of 2 in the M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of M296I Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna and Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1031 b:75.3 occ:1.00 O A:TYR241 3.1 48.9 1.0 N A:TYR241 3.3 47.1 1.0 O A:HOH484 3.7 32.2 1.0 OD2 A:ASP338 3.8 48.3 1.0 C A:TYR241 3.8 48.7 1.0 CA A:TYR241 4.0 47.2 1.0 CG A:ASP338 4.1 44.2 1.0 CB A:TYR241 4.2 46.1 1.0 C A:ASP240 4.3 48.1 1.0 CA A:ASP240 4.3 48.3 1.0 CB A:ASP240 4.4 50.0 1.0 OD1 A:ASP240 4.4 52.3 1.0 CB A:ASP338 4.5 42.5 1.0 CG A:ASP240 4.6 51.1 1.0 OD1 A:ASP338 4.6 48.3 1.0 O A:ASP338 4.7 41.3 1.0 C A:ASP338 5.0 40.4 1.0

C.Ferrer-Orta, M.Sierra, R.Agudo, I.De La Higuera, A.Arias, R.Perez-Luque, C.Escarmis, E.Domingo, N.Verdaguer. Structure of Foot-and-Mouth Disease Virus Mutant Polymerases with Reduced Sensitivity to Ribavirin J.Virol. V. 84 6188 2010.
ISSN: ISSN 0022-538X
PubMed: 20392853
DOI: 10.1128/JVI.02420-09