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Magnesium in PDB 5cyr: Crystal Structure of Thosea Asigna Virus Rna-Dependent Rna Polymerase (Rdrp) Complexed with Atp and Ssrna

Protein crystallography data

The structure of Crystal Structure of Thosea Asigna Virus Rna-Dependent Rna Polymerase (Rdrp) Complexed with Atp and Ssrna, PDB code: 5cyr was solved by D.S.Ferrero, M.Buxaderas, J.F.Rodriguez, N.Verdaguer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.60 / 3.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 142.513, 158.339, 217.096, 90.00, 90.00, 90.00
R / Rfree (%) 25.2 / 29.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Thosea Asigna Virus Rna-Dependent Rna Polymerase (Rdrp) Complexed with Atp and Ssrna (pdb code 5cyr). 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 Crystal Structure of Thosea Asigna Virus Rna-Dependent Rna Polymerase (Rdrp) Complexed with Atp and Ssrna, PDB code: 5cyr:

Magnesium binding site 1 out of 1 in 5cyr

Go back to Magnesium Binding Sites List in 5cyr
Magnesium binding site 1 out of 1 in the Crystal Structure of Thosea Asigna Virus Rna-Dependent Rna Polymerase (Rdrp) Complexed with Atp and Ssrna


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Thosea Asigna Virus Rna-Dependent Rna Polymerase (Rdrp) Complexed with Atp and Ssrna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg701

b:18.8
occ:1.00
NZ A:LYS36 2.2 42.8 1.0
NH2 A:ARG35 2.7 48.5 1.0
CE A:LYS36 3.6 32.6 1.0
CZ A:ARG35 4.0 51.2 1.0
NH1 A:ARG22 4.1 29.5 1.0
CD A:LYS36 4.7 44.4 1.0
NE A:ARG35 4.8 46.1 1.0
NH1 A:ARG35 4.8 50.3 1.0
CG A:LYS36 4.9 46.6 1.0
CE1 B:HIS102 4.9 45.5 1.0

Reference:

D.S.Ferrero, M.Buxaderas, J.F.Rodriguez, N.Verdaguer. The Structure of the Rna-Dependent Rna Polymerase of A Permutotetravirus Suggests A Link Between Primer-Dependent and Primer-Independent Polymerases. Plos Pathog. V. 11 05265 2015.
ISSN: ESSN 1553-7374
PubMed: 26625123
DOI: 10.1371/JOURNAL.PPAT.1005265
Page generated: Sun Sep 29 02:19:57 2024

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