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Magnesium in PDB 3kms: G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure

Enzymatic activity of G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure

All present enzymatic activity of G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure:
2.7.7.48;

Protein crystallography data

The structure of G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure, PDB code: 3kms 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) 29.40 / 2.20
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 93.951, 93.951, 99.997, 90.00, 90.00, 120.00
R / Rfree (%) 23.6 / 26.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure (pdb code 3kms). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure, PDB code: 3kms:

Magnesium binding site 1 out of 1 in 3kms

Go back to Magnesium Binding Sites List in 3kms
Magnesium binding site 1 out of 1 in the G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of G62S Mutant of Foot-and-Mouth Disease Virus Rna-Polymerase in Complex with A Template- Primer Rna Trigonal Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg950

b:67.3
occ:1.00
OD2 A:ASP238 2.4 51.0 1.0
OD1 A:ASP240 2.9 51.1 1.0
CG A:ASP238 3.4 50.2 1.0
OD1 A:ASP238 3.7 50.4 1.0
OD1 A:ASP339 3.7 50.2 1.0
CB A:ALA367 3.8 58.2 1.0
O A:THR384 3.9 49.0 1.0
CG A:ASP240 4.0 50.6 1.0
O A:VAL239 4.1 50.0 1.0
OD2 A:ASP240 4.6 51.5 1.0
C A:VAL239 4.6 49.8 1.0
O A:HOH608 4.7 42.9 1.0
CB A:ASP238 4.7 49.6 1.0
O A:ILE340 4.7 48.5 1.0
N A:VAL239 4.8 49.7 1.0
CG A:ASP339 4.8 49.1 1.0
C A:THR384 4.8 48.9 1.0
C A:ASP238 4.8 49.5 1.0

Reference:

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
Page generated: Mon Dec 14 08:22:51 2020

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