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Magnesium in PDB 3fqi: Crystal Structure of the Mouse DOM3Z

Protein crystallography data

The structure of Crystal Structure of the Mouse DOM3Z, PDB code: 3fqi 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) 30.00 / 2.01
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.979, 88.379, 50.069, 90.00, 114.20, 90.00
R / Rfree (%) 22.6 / 28.3

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 3fqi

Go back to Magnesium Binding Sites List in 3fqi
Magnesium binding site 1 out of 1 in the Crystal Structure of the Mouse DOM3Z


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1000

b:17.7
occ:1.00
O A:HOH638 2.0 30.0 1.0
O A:HOH637 2.2 26.5 1.0
OE2 A:GLU253 2.2 17.6 1.0
OD2 A:ASP236 2.3 14.9 1.0
O A:LEU254 2.4 11.3 1.0
O A:HOH600 2.4 23.3 1.0
CD A:GLU253 3.2 16.3 1.0
CG A:ASP236 3.2 14.3 1.0
OD1 A:ASP236 3.4 16.0 1.0
C A:LEU254 3.5 11.9 1.0
N A:LEU254 3.8 11.6 1.0
NZ A:LYS255 3.9 15.1 1.0
CG A:GLU253 4.0 13.5 1.0
CD A:LYS255 4.1 13.3 1.0
OE1 A:GLU253 4.1 17.1 1.0
CA A:LEU254 4.2 11.8 1.0
CE A:LYS255 4.2 14.7 1.0
OE2 A:GLU192 4.4 20.4 1.0
O A:HOH451 4.5 20.2 1.0
CB A:LEU254 4.6 12.1 1.0
CB A:ASP236 4.6 12.9 1.0
N A:LYS255 4.7 12.3 1.0
C A:GLU253 4.8 11.9 1.0
CG A:LYS255 4.9 13.8 1.0
NE2 A:GLN280 4.9 19.7 1.0
CA A:LYS255 5.0 13.0 1.0
CA A:GLU253 5.0 11.9 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: Wed Aug 14 13:51:51 2024

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