Magnesium in PDB 3nl0: Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase

The structure of Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase, PDB code: 3nl0 was solved by R.Agudo, C.Ferrer-Orta, A.Arias, R.Perez-Luque, N.Verdaguer, E.Domingo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.32 / 2.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	93.713, 93.713, 99.723, 90.00, 90.00, 120.00
R / Rfree (%)	22.6 / 27.4

The binding sites of Magnesium atom in the Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase (pdb code 3nl0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase, PDB code: 3nl0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1055 b:72.1 occ:1.00 OD2 A:ASP238 2.6 50.3 1.0 OD1 A:ASP339 3.0 44.6 1.0 O A:THR384 3.1 49.9 1.0 OD2 A:ASP240 3.3 48.0 1.0 CG A:ASP238 3.6 50.8 1.0 OD1 A:ASP238 3.9 51.5 1.0 CG A:ASP339 4.1 43.2 1.0 C A:THR384 4.3 49.9 1.0 O A:VAL239 4.3 47.0 1.0 O A:ILE340 4.5 45.9 1.0 CB A:ALA367 4.5 63.8 1.0 CG A:ASP240 4.5 49.3 1.0 OD2 A:ASP339 4.7 43.7 1.0 N A:ILE340 4.8 43.8 1.0 CB A:ASP238 4.9 51.5 1.0

Magnesium binding site 2 out of 2 in the Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mutant P44S M296I of Foot-and-Mouth Disease Virus Rna-Dependent Rna Polymerase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1056 b:61.5 occ:1.00 OP1 B:G905 2.8 0.9 0.8 NH1 A:ARG128 3.0 55.9 1.0 N A:GLU112 3.3 56.9 1.0 C5' B:G905 3.4 0.4 0.8 CA A:MET111 3.6 55.8 1.0 OP2 B:G906 3.7 0.4 0.8 CB A:MET111 3.7 56.6 1.0 P B:G905 3.7 1.0 0.8 CG A:MET111 3.8 55.5 1.0 NH2 A:ARG128 3.9 56.0 1.0 CZ A:ARG128 3.9 56.8 1.0 O5' B:G905 4.0 0.4 0.8 C A:MET111 4.0 56.9 1.0 OP2 B:G905 4.2 0.5 0.8 CB A:GLU112 4.4 57.5 1.0 CA A:GLU112 4.4 58.2 1.0 CG2 A:ILE189 4.4 46.6 1.0 O A:GLU112 4.5 60.1 1.0 CE A:MET111 4.6 56.6 1.0 OG1 A:THR115 4.6 58.6 1.0 C4' B:G905 4.6 0.3 0.8 P B:G906 4.7 0.8 0.8 C3' B:G905 4.8 0.2 0.8 O3' B:G905 4.8 0.6 0.8 N A:MET111 4.9 55.5 1.0 C A:GLU112 4.9 59.9 1.0 CG A:GLU112 5.0 57.2 1.0

R.Agudo, C.Ferrer-Orta, A.Arias, I.De La Higuera, C.Perales, R.Perez-Luque, N.Verdaguer, E.Domingo. A Multi-Step Process of Viral Adaptation to A Mutagenic Nucleoside Analogue By Modulation of Transition Types Leads to Extinction-Escape. Plos Pathog. V. 6 01072 2010.
ISSN: ISSN 1553-7366
PubMed: 20865120
DOI: 10.1371/JOURNAL.PPAT.1001072