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Magnesium in PDB 4nyz: The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution

Enzymatic activity of The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution

All present enzymatic activity of The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution:
2.7.7.48; 3.4.22.28; 3.6.1.15;

Protein crystallography data

The structure of The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution, PDB code: 4nyz was solved by L.Vives-Adrian, C.Lujan, C.Ferrer-Orta, N.Verdaguer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 104.30 / 2.15
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 122.553, 122.553, 198.797, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution (pdb code 4nyz). 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 The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution, PDB code: 4nyz:

Magnesium binding site 1 out of 1 in 4nyz

Go back to Magnesium Binding Sites List in 4nyz
Magnesium binding site 1 out of 1 in the The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Emcv 3DPOL Structure with Altered Motif A Conformation at 2.15A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:31.8
occ:1.00
OE2 A:GLU161 2.7 25.6 1.0
O A:LYS159 2.8 28.2 1.0
N A:ARG174 3.0 26.4 1.0
CG A:GLU161 3.3 26.2 1.0
CG2 A:THR173 3.4 27.1 1.0
CD A:GLU161 3.4 25.8 1.0
CB A:ALA36 3.6 23.8 1.0
CD A:ARG163 3.6 27.8 1.0
CB A:ARG174 3.7 26.4 1.0
CB A:LYS159 3.7 29.6 1.0
C A:LYS159 3.8 29.3 1.0
CA A:ARG174 3.8 26.9 1.0
CA A:THR173 3.8 26.4 1.0
C A:THR173 3.9 26.3 1.0
CG A:ARG163 3.9 27.3 1.0
O A:ARG174 4.0 28.6 1.0
CG A:ARG174 4.1 26.1 1.0
CB A:THR173 4.2 27.0 1.0
NE A:ARG163 4.2 28.1 1.0
CA A:LYS159 4.2 29.8 1.0
C A:ARG174 4.3 28.1 1.0
N A:LYS159 4.5 30.0 1.0
CG A:LYS159 4.5 29.9 1.0
OE1 A:GLU161 4.6 25.7 1.0
CB A:GLU161 4.7 26.5 1.0
N A:GLU161 4.8 27.8 1.0
NE A:ARG174 4.8 26.3 1.0
OG1 A:THR173 4.9 27.3 1.0
CD A:LYS159 4.9 29.9 1.0
O A:GLU161 4.9 26.5 1.0
N A:ASP160 5.0 29.6 1.0

Reference:

L.Vives-Adrian, C.Lujan, B.Oliva, L.Van Der Linden, B.Selisko, B.Coutard, B.Canard, F.J.Van Kuppeveld, C.Ferrer-Orta, N.Verdaguer. The Crystal Structure of A Cardiovirus Rna-Dependent Rna Polymerase Reveals An Unusual Conformation of the Polymerase Active Site J.Virol. 2014.
ISSN: ESSN 1098-5514
PubMed: 24600002
DOI: 10.1128/JVI.03502-13
Page generated: Mon Dec 14 19:16:08 2020

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