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Magnesium in PDB 2fbx: Wrn Exonuclease, Mg Complex

Protein crystallography data

The structure of Wrn Exonuclease, Mg Complex, PDB code: 2fbx was solved by J.J.Perry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.70 / 2.20
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.806, 80.806, 93.174, 90.00, 90.00, 120.00
R / Rfree (%) 24.2 / 26.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Wrn Exonuclease, Mg Complex (pdb code 2fbx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Wrn Exonuclease, Mg Complex, PDB code: 2fbx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2fbx

Go back to Magnesium Binding Sites List in 2fbx
Magnesium binding site 1 out of 2 in the Wrn Exonuclease, Mg Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Wrn Exonuclease, Mg Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg237

b:45.6
occ:0.50
OD2 A:ASP82 2.7 49.0 1.0
O A:HOH418 2.9 46.9 1.0
MG A:MG238 3.4 57.0 1.0
CG A:ASP82 3.7 43.9 1.0
O A:MET83 3.8 36.3 1.0
OD1 A:ASP82 3.9 49.0 1.0
N A:MET83 4.7 35.7 1.0
OD1 A:ASP143 4.7 40.8 1.0
OE2 A:GLU84 4.8 38.0 1.0
CH2 A:TRP85 4.9 37.1 1.0
C A:MET83 4.9 35.5 1.0

Magnesium binding site 2 out of 2 in 2fbx

Go back to Magnesium Binding Sites List in 2fbx
Magnesium binding site 2 out of 2 in the Wrn Exonuclease, Mg Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Wrn Exonuclease, Mg Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg238

b:57.0
occ:1.00
OE2 A:GLU84 2.5 38.0 1.0
OD2 A:ASP216 2.7 32.2 1.0
OD1 A:ASP82 3.0 49.0 1.0
CD A:GLU84 3.3 38.8 1.0
MG A:MG237 3.4 45.6 0.5
OE1 A:GLU84 3.5 38.0 1.0
CG A:ASP82 3.6 43.9 1.0
CG A:ASP216 3.6 36.6 1.0
OD2 A:ASP82 3.6 49.0 1.0
O A:HOH440 3.8 37.4 1.0
NH2 A:ARG196 3.9 51.1 1.0
CB A:ASP216 3.9 35.6 1.0
O A:MET83 4.2 36.3 1.0
NE2 A:GLN101 4.6 36.1 1.0
OD1 A:ASP216 4.7 38.8 1.0
CG A:GLU84 4.8 38.6 1.0
CB A:ASP82 4.8 40.5 1.0

Reference:

J.J.Perry, S.M.Yannone, L.G.Holden, C.Hitomi, A.Asaithamby, S.Han, P.K.Cooper, D.J.Chen, J.A.Tainer. Wrn Exonuclease Structure and Molecular Mechanism Imply An Editing Role in Dna End Processing. Nat.Struct.Mol.Biol. V. 13 414 2006.
ISSN: ISSN 1545-9993
PubMed: 16622405
DOI: 10.1038/NSMB1088
Page generated: Mon Dec 14 07:22:43 2020

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