Magnesium in PDB 5f8h: Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form)

All present enzymatic activity of Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form):
2.7.7.48;

The structure of Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form), PDB code: 5f8h was solved by B.Shu, P.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.96 / 2.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.344, 77.081, 149.853, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.4

The structure of Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form) (pdb code 5f8h). 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 Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form), PDB code: 5f8h:

Magnesium binding site 1 out of 1 in the Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Enterovirus 71 Polymerase Elongation Complex (C1S1/2 Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:45.6 occ:0.67 O A:HOH649 1.9 43.6 1.0 O A:HOH639 2.0 56.0 1.0 OD1 A:ASP330 2.2 42.7 1.0 O A:HOH693 2.2 47.0 1.0 O A:HOH606 2.5 58.5 1.0 O A:HOH603 2.7 45.9 1.0 CG A:ASP330 3.2 38.3 1.0 O A:HOH648 3.5 41.2 1.0 OD2 A:ASP330 3.7 38.1 1.0 OD1 A:ASP233 3.9 49.5 1.0 O A:THR373 3.9 39.6 1.0 OG1 A:THR373 4.0 49.5 1.0 CA A:PHE374 4.3 35.1 1.0 C A:THR373 4.4 41.6 1.0 O A:HOH698 4.5 51.1 1.0 O A:HOH655 4.5 48.1 1.0 CB A:ASP330 4.5 39.4 1.0 O A:VAL331 4.6 43.5 1.0 O A:HOH706 4.6 51.6 1.0 N A:PHE374 4.6 36.3 1.0 CA A:ASP330 4.7 42.3 1.0 N A:VAL331 4.7 40.3 1.0 N A:LEU375 4.8 36.5 1.0 CD1 A:PHE374 4.9 37.3 1.0

B.Shu, P.Gong. Structural Basis of Viral Rna-Dependent Rna Polymerase Catalysis and Translocation Proc.Natl.Acad.Sci.Usa V. 113 E4005 2016.
ISSN: ESSN 1091-6490
PubMed: 27339134
DOI: 10.1073/PNAS.1602591113