Magnesium in PDB 2ec0: Rna-Dependent Rna Polymerase of Foot-and-Mouth Disease Virus in Complex with A Template-Primer Rna and Atp

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

The structure of Rna-Dependent Rna Polymerase of Foot-and-Mouth Disease Virus in Complex with A Template-Primer Rna and Atp, PDB code: 2ec0 was solved by C.Ferrer-Orta, A.Arias, R.Perez-Luque, C.Escarmis, E.Domingo, N.Verdaguer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.75
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.656, 95.656, 201.458, 90.00, 90.00, 120.00
R / Rfree (%)	24.5 / 29.5

The binding sites of Magnesium atom in the Rna-Dependent Rna Polymerase of Foot-and-Mouth Disease Virus in Complex with A Template-Primer Rna and Atp (pdb code 2ec0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Rna-Dependent Rna Polymerase of Foot-and-Mouth Disease Virus in Complex with A Template-Primer Rna and Atp, PDB code: 2ec0:
Jump to Magnesium binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rna-Dependent Rna Polymerase of Foot-and-Mouth Disease Virus in Complex with A Template-Primer Rna and Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1990 b:44.5 occ:1.00 O A:HOH962 2.2 46.5 1.0 O A:HOH963 2.3 16.1 1.0 OD1 A:ASP339 2.5 44.7 1.0 OD1 A:ASP238 2.7 53.2 1.0 O A:THR384 2.8 43.8 1.0 CG A:ASP339 3.5 43.1 1.0 C A:THR384 3.8 43.9 1.0 CG A:ASP238 3.8 52.2 1.0 OD2 A:ASP339 3.9 41.8 1.0 O A:ILE340 4.2 44.4 1.0 CG2 A:THR384 4.2 45.3 1.0 OD2 A:ASP238 4.2 52.5 1.0 CA A:PHE385 4.4 41.5 1.0 N A:ILE340 4.5 43.8 1.0 OD1 A:ASP240 4.5 47.7 1.0 N A:PHE385 4.5 42.5 1.0 CB A:THR384 4.6 44.7 1.0 O A:HOH952 4.6 43.6 1.0 CA A:THR384 4.7 44.6 1.0 O A:VAL239 4.7 48.3 1.0 CB A:ASP339 4.7 43.2 1.0 CA A:ASP339 4.9 43.5 1.0 CD1 A:PHE385 4.9 39.0 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Rna-Dependent Rna Polymerase of Foot-and-Mouth Disease Virus in Complex with A Template-Primer Rna and Atp within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg3990 b:47.3 occ:1.00 O D:HOH2964 2.2 33.2 1.0 O D:HOH2963 2.5 46.1 1.0 OD1 D:ASP339 2.6 44.6 1.0 OD1 D:ASP238 2.9 53.3 1.0 O D:THR384 3.1 43.7 1.0 CG D:ASP339 3.5 42.9 1.0 OD2 D:ASP339 3.9 41.1 1.0 CG D:ASP238 4.0 52.2 1.0 C D:THR384 4.0 43.9 1.0 OD1 D:ASP240 4.1 46.9 1.0 OD2 D:ASP238 4.4 53.5 1.0 CG2 D:THR384 4.4 44.8 1.0 O D:ILE340 4.4 44.3 1.0 O D:HOH2952 4.5 50.2 1.0 N D:ILE340 4.6 43.9 1.0 O D:VAL239 4.7 48.3 1.0 CA D:PHE385 4.7 41.5 1.0 CB D:THR384 4.7 44.9 1.0 CB D:ASP339 4.8 43.2 1.0 N D:PHE385 4.8 42.7 1.0 CA D:ASP339 4.8 43.5 1.0 CA D:THR384 4.9 44.6 1.0

C.Ferrer-Orta, A.Arias, R.Perez-Luque, C.Escarmis, E.Domingo, N.Verdaguer. Sequential Structures Provide Insights Into the Fidelity of Rna Replication Proc.Natl.Acad.Sci.Usa V. 104 9463 2007.
ISSN: ISSN 0027-8424
PubMed: 17517631
DOI: 10.1073/PNAS.0700518104