Atomistry » Magnesium » PDB 4a35-4aas » 4a8q
Atomistry »
  Magnesium »
    PDB 4a35-4aas »
      4a8q »

Magnesium in PDB 4a8q: Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation

Protein crystallography data

The structure of Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation, PDB code: 4a8q was solved by S.Wright, M.M.Poranen, D.H.Bamford, D.I.Stuart, J.M.Grimes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 77.07 / 3.06
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 107.440, 92.850, 141.230, 90.00, 101.85, 90.00
R / Rfree (%) 20.48 / 22.01

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation (pdb code 4a8q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation, PDB code: 4a8q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4a8q

Go back to Magnesium Binding Sites List in 4a8q
Magnesium binding site 1 out of 2 in the Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1665

b:64.8
occ:1.00
OE1 A:GLU491 2.1 63.1 1.0
OD1 A:ASP454 2.2 80.0 1.0
O A:ALA495 2.6 58.2 1.0
CD A:GLU491 3.0 79.3 1.0
CG A:ASP454 3.3 77.3 1.0
OE2 A:GLU491 3.5 71.4 1.0
O A:THR323 3.5 70.0 1.0
C A:ALA495 3.8 58.4 1.0
OD2 A:ASP454 3.9 81.8 1.0
CG A:GLU491 4.2 69.1 1.0
O A:ALA455 4.3 62.3 1.0
CB A:GLU491 4.3 62.5 1.0
N A:ALA495 4.4 55.7 1.0
CB A:ASP454 4.4 64.1 1.0
N A:ALA455 4.4 60.0 1.0
CA A:ASP454 4.5 62.4 1.0
CA A:ALA495 4.6 54.3 1.0
C A:THR323 4.7 69.4 1.0
N A:PHE496 4.7 54.9 1.0
CA A:PHE496 4.8 53.7 1.0
C A:ASP454 5.0 65.0 1.0

Magnesium binding site 2 out of 2 in 4a8q

Go back to Magnesium Binding Sites List in 4a8q
Magnesium binding site 2 out of 2 in the Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Non-Catalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Dsrna Virus PHI6 From De Novo Initiation to Elongation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1665

b:57.9
occ:1.00
OE1 B:GLU491 2.1 80.0 1.0
OD1 B:ASP454 2.2 71.3 1.0
O B:ALA495 2.6 56.0 1.0
CD B:GLU491 3.0 91.5 1.0
CG B:ASP454 3.3 68.0 1.0
OE2 B:GLU491 3.4 91.4 1.0
O B:THR323 3.6 62.7 1.0
C B:ALA495 3.8 57.3 1.0
OD2 B:ASP454 3.9 68.7 1.0
CG B:GLU491 4.2 71.0 1.0
O B:ALA455 4.2 58.0 1.0
CB B:GLU491 4.4 62.4 1.0
N B:ALA495 4.4 54.6 1.0
CB B:ASP454 4.5 58.5 1.0
N B:ALA455 4.5 55.8 1.0
CA B:ASP454 4.5 56.4 1.0
CA B:ALA495 4.6 54.5 1.0
N B:PHE496 4.8 53.5 1.0
CA B:PHE496 4.8 52.7 1.0
C B:THR323 4.8 62.1 1.0
C B:ASP454 5.0 60.4 1.0

Reference:

S.Wright, M.M.Poranen, D.H.Bamford, D.I.Stuart, J.M.Grimes. Noncatalytic Ions Direct the Rna-Dependent Rna Polymerase of Bacterial Double-Stranded Rna Virus PHI6 From De Novo Initiation to Elongation. J.Virol. V. 86 2837 2012.
ISSN: ISSN 0022-538X
PubMed: 22205747
DOI: 10.1128/JVI.05168-11
Page generated: Thu Aug 15 14:23:46 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy