Magnesium in PDB 2e9z: Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, Atp and Utp

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

The structure of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, Atp and Utp, PDB code: 2e9z 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)	30.00 / 3.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.110, 94.110, 99.362, 90.00, 90.00, 120.00
R / Rfree (%)	22.7 / 29

The binding sites of Magnesium atom in the Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, Atp and Utp (pdb code 2e9z). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, Atp and Utp, PDB code: 2e9z:
Jump to Magnesium binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, Atp and Utp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1030 b:27.1 occ:1.00 OD1 A:ASP238 2.8 57.1 1.0 OD2 A:ASP339 2.9 40.9 1.0 O A:THR384 3.1 39.0 1.0 OD1 A:ASP339 3.2 45.3 1.0 CG A:ASP339 3.3 42.4 1.0 CG A:ASP238 3.7 54.7 1.0 OD1 A:ASP240 3.9 35.9 1.0 OD2 A:ASP238 3.9 55.1 1.0 O A:VAL239 4.1 39.9 1.0 C A:THR384 4.3 38.8 1.0 O A:ILE340 4.5 39.8 1.0 CB A:ASP339 4.6 41.4 1.0 CG A:ASP240 4.6 34.4 1.0 CB A:ALA367 4.8 66.1 1.0 OD2 A:ASP240 4.8 37.3 1.0 CA A:ASP339 4.8 42.1 1.0 N A:ILE340 4.9 42.2 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna, Atp and Utp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1031 b:73.1 occ:1.00 O3A A:UTP993 2.9 97.0 0.5 O A:TYR241 3.1 42.1 1.0 O3B A:UTP993 3.4 94.9 0.5 PB A:UTP993 3.8 95.8 0.5 OD2 A:ASP338 4.0 37.3 1.0 PA A:UTP993 4.0 98.7 0.5 O2A A:UTP993 4.0 98.6 0.5 O1G A:UTP993 4.1 94.2 0.5 C A:TYR241 4.3 40.9 1.0 PG A:UTP993 4.4 94.3 0.5 O1B A:UTP993 4.6 95.3 0.5 N A:TYR241 4.6 37.4 1.0 OD2 A:ASP240 4.6 37.3 1.0 O2G A:UTP993 4.8 94.1 0.6 O5' A:UTP993 4.8 98.5 0.5

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