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Magnesium in PDB 3fqj: Crystal Structure of the Mouse DOM3Z in Complex with Gdp

Protein crystallography data

The structure of Crystal Structure of the Mouse DOM3Z in Complex with Gdp, PDB code: 3fqj was solved by S.Xiang, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.15 / 2.62
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.293, 73.573, 108.890, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 26.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Mouse DOM3Z in Complex with Gdp (pdb code 3fqj). 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 the Mouse DOM3Z in Complex with Gdp, PDB code: 3fqj:

Magnesium binding site 1 out of 1 in 3fqj

Go back to Magnesium Binding Sites List in 3fqj
Magnesium binding site 1 out of 1 in the Crystal Structure of the Mouse DOM3Z in Complex with Gdp


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 Mouse DOM3Z in Complex with Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1000

b:26.5
occ:1.00
OD2 A:ASP236 2.6 25.6 1.0
NZ A:LYS255 2.9 20.8 1.0
O A:LEU254 3.0 21.2 1.0
OE2 A:GLU253 3.3 19.7 1.0
OE2 A:GLU192 3.3 25.7 1.0
CG A:ASP236 3.4 23.9 1.0
OD1 A:ASP236 3.5 24.3 1.0
CD A:LYS255 3.7 21.1 1.0
CE A:LYS255 3.8 20.4 1.0
CD A:GLU253 3.8 19.4 1.0
O A:HOH492 4.0 18.7 1.0
C A:LEU254 4.1 21.2 1.0
CG A:GLU253 4.1 19.0 1.0
N A:LEU254 4.4 20.2 1.0
CD A:GLU192 4.6 24.0 1.0
OE1 A:GLU253 4.6 20.1 1.0
O A:HOH485 4.7 24.6 1.0
CB A:ASP236 4.8 22.6 1.0
CA A:LEU254 4.8 20.8 1.0
O A:HOH430 4.9 33.9 1.0
OE1 A:GLN280 4.9 16.6 1.0
CG A:LYS255 4.9 21.5 1.0

Reference:

S.Xiang, A.Cooper-Morgan, X.Jiao, M.Kiledjian, J.L.Manley, L.Tong. Structure and Function of the 5'-->3' Exoribonuclease RAT1 and Its Activating Partner RAI1. Nature V. 458 784 2009.
ISSN: ISSN 0028-0836
PubMed: 19194460
DOI: 10.1038/NATURE07731
Page generated: Mon Dec 14 08:09:05 2020

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