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Magnesium in PDB 2y35: Crystal Structure of XRN1-Substrate Complex

Protein crystallography data

The structure of Crystal Structure of XRN1-Substrate Complex, PDB code: 2y35 was solved by M.Jinek, S.M.Coyle, J.A.Doudna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 74.995 / 3.20
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 149.990, 149.990, 154.860, 90.00, 90.00, 90.00
R / Rfree (%) 22.46 / 27.11

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of XRN1-Substrate Complex (pdb code 2y35). 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 XRN1-Substrate Complex, PDB code: 2y35:

Magnesium binding site 1 out of 1 in 2y35

Go back to Magnesium Binding Sites List in 2y35
Magnesium binding site 1 out of 1 in the Crystal Structure of XRN1-Substrate Complex


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 XRN1-Substrate Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2141

b:69.4
occ:1.00
O A:HOH2003 2.1 58.5 1.0
OE1 A:GLU177 2.1 85.2 1.0
O A:HOH2002 2.1 0.9 1.0
O A:HOH2005 2.1 64.5 1.0
O A:HOH2004 2.1 92.8 1.0
O A:HOH2006 2.1 46.6 1.0
CD A:GLU177 3.2 84.9 1.0
OD2 A:ASP86 3.7 85.6 1.0
OD2 A:ASP35 3.8 81.5 1.0
OD1 A:ASP86 3.8 84.9 1.0
CG A:GLU177 3.9 84.8 1.0
CG A:ASP86 4.2 85.6 1.0
CB A:GLU177 4.2 84.5 1.0
OE2 A:GLU177 4.2 84.7 1.0
OE1 A:GLU175 4.5 86.8 1.0
N A:GLU177 4.5 52.7 1.0
OP1 B:DT2 4.5 0.8 1.0
CG A:ASP35 4.6 81.7 1.0
OD1 A:ASP35 4.7 82.2 1.0
CB A:GLU175 4.7 87.6 1.0
O3' B:DT1 4.7 0.4 1.0
CD A:GLU175 5.0 87.5 1.0
N A:GLY176 5.0 52.6 1.0

Reference:

M.Jinek, S.M.Coyle, J.A.Doudna. Coupled 5' Nucleotide Recognition and Processivity in XRN1-Mediated Mrna Decay. Mol.Cell V. 41 600 2011.
ISSN: ISSN 1097-2765
PubMed: 21362555
DOI: 10.1016/J.MOLCEL.2011.02.004
Page generated: Mon Dec 14 07:47:56 2020

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