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Magnesium in PDB 4rwo: Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position

Enzymatic activity of Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position

All present enzymatic activity of Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position:
2.7.7.84;

Protein crystallography data

The structure of Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position, PDB code: 4rwo was solved by J.Lohoefener, N.Steinke, P.Kay-Fedorov, P.Baruch, A.Nikulin, S.Tishchenko, D.J.Manstein, R.Fedorov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.31 / 2.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.100, 73.100, 208.420, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position (pdb code 4rwo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position, PDB code: 4rwo:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4rwo

Go back to Magnesium Binding Sites List in 4rwo
Magnesium binding site 1 out of 2 in the Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position


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 the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:67.6
occ:1.00
O A:HOH543 1.9 53.7 1.0
O2B A:APC403 1.9 69.9 0.9
O2A A:APC403 2.0 66.6 0.9
O2G A:APC403 2.0 67.0 0.9
OD1 A:ASP74 2.0 75.1 1.0
OD2 A:ASP76 2.2 67.1 1.0
PB A:APC403 3.0 51.4 0.9
CG A:ASP74 3.1 73.3 1.0
CG A:ASP76 3.2 70.2 1.0
PA A:APC403 3.2 55.2 0.9
PG A:APC403 3.3 50.4 0.9
OD2 A:ASP74 3.4 84.4 1.0
C3A A:APC403 3.5 45.7 0.9
MG A:MG402 3.5 70.2 1.0
OD1 A:ASP76 3.5 82.8 1.0
O3B A:APC403 3.6 51.4 0.9
O A:HOH553 3.8 59.1 1.0
OG A:SER62 3.8 55.5 1.0
C5' A:APC403 4.0 64.2 0.9
O3G A:APC403 4.0 51.4 0.9
O5' A:APC403 4.1 64.6 0.9
N A:SER62 4.1 55.8 1.0
O A:ASP74 4.1 60.3 1.0
O A:HOH544 4.2 54.5 1.0
O1B A:APC403 4.3 57.6 0.9
O1G A:APC403 4.4 41.9 0.9
CB A:ASP74 4.4 68.7 1.0
O1A A:APC403 4.4 58.6 0.9
N A:ASP74 4.5 63.0 1.0
CA A:GLY61 4.5 50.0 1.0
CB A:ASP76 4.5 68.4 1.0
C A:ASP74 4.5 67.0 1.0
CB A:SER62 4.7 42.9 1.0
CA A:ASP74 4.7 60.6 1.0
C A:GLY61 4.9 54.7 1.0

Magnesium binding site 2 out of 2 in 4rwo

Go back to Magnesium Binding Sites List in 4rwo
Magnesium binding site 2 out of 2 in the Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Porcine OAS1 L149R Mutant in Complex with Dsrna and Apcpp in the Amp Donor Position within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:70.2
occ:1.00
OD1 A:ASP76 2.0 82.8 1.0
O2A A:APC403 2.4 66.6 0.9
OD2 A:ASP74 2.5 84.4 1.0
CG A:ASP76 3.0 70.2 1.0
OD2 A:ASP147 3.1 79.8 1.0
OD2 A:ASP76 3.4 67.1 1.0
CG A:ASP74 3.4 73.3 1.0
PA A:APC403 3.5 55.2 0.9
MG A:MG401 3.5 67.6 1.0
OD1 A:ASP74 3.6 75.1 1.0
CG A:ASP147 3.7 83.1 1.0
O1A A:APC403 3.8 58.6 0.9
CB A:ASP147 3.9 72.7 1.0
O5' A:APC403 4.0 64.6 0.9
C5' A:APC403 4.0 64.2 0.9
CB A:ASP76 4.3 68.4 1.0
OD1 A:ASP147 4.7 82.2 1.0
CB A:ASP74 4.7 68.7 1.0
O2B A:APC403 4.8 69.9 0.9
O2G A:APC403 4.9 67.0 0.9
NH2 A:ARG149 5.0 72.3 1.0
CA A:ASP76 5.0 62.9 1.0

Reference:

J.Lohofener, N.Steinke, P.Kay-Fedorov, P.Baruch, A.Nikulin, S.Tishchenko, D.J.Manstein, R.Fedorov. The Activation Mechanism of 2'-5'-Oligoadenylate Synthetase Gives New Insights Into Oas/Cgas Triggers of Innate Immunity. Structure V. 23 851 2015.
ISSN: ISSN 0969-2126
PubMed: 25892109
DOI: 10.1016/J.STR.2015.03.012
Page generated: Mon Dec 14 19:32:31 2020

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