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Magnesium in PDB 4ofh: Structural Basis For Thymine Glycosylase Activity on T:O6-Methylg Mismatch By Methyl-Cpg Binding Domain Protein 4: Implications For Roles of ARG468 in Mismatch Recognition and Catalysis

Protein crystallography data

The structure of Structural Basis For Thymine Glycosylase Activity on T:O6-Methylg Mismatch By Methyl-Cpg Binding Domain Protein 4: Implications For Roles of ARG468 in Mismatch Recognition and Catalysis, PDB code: 4ofh was solved by H.Ouzon-Shubeita, Y.-L.Lin, S.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.83 / 2.22
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.983, 57.640, 105.100, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 23

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Basis For Thymine Glycosylase Activity on T:O6-Methylg Mismatch By Methyl-Cpg Binding Domain Protein 4: Implications For Roles of ARG468 in Mismatch Recognition and Catalysis (pdb code 4ofh). 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 Structural Basis For Thymine Glycosylase Activity on T:O6-Methylg Mismatch By Methyl-Cpg Binding Domain Protein 4: Implications For Roles of ARG468 in Mismatch Recognition and Catalysis, PDB code: 4ofh:

Magnesium binding site 1 out of 1 in 4ofh

Go back to Magnesium Binding Sites List in 4ofh
Magnesium binding site 1 out of 1 in the Structural Basis For Thymine Glycosylase Activity on T:O6-Methylg Mismatch By Methyl-Cpg Binding Domain Protein 4: Implications For Roles of ARG468 in Mismatch Recognition and Catalysis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For Thymine Glycosylase Activity on T:O6-Methylg Mismatch By Methyl-Cpg Binding Domain Protein 4: Implications For Roles of ARG468 in Mismatch Recognition and Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:30.6
occ:1.00
O A:LEU534 2.3 25.7 1.0
O A:ILE532 2.4 26.6 1.0
O C:HOH118 2.4 26.9 1.0
O A:ILE537 2.5 26.3 1.0
O C:HOH102 2.6 34.1 1.0
OP1 C:DA10 2.6 28.5 1.0
C A:LEU534 3.2 26.5 1.0
C A:ILE532 3.4 25.3 1.0
C A:ILE537 3.6 25.4 1.0
N A:LEU534 3.8 29.8 1.0
P C:DA10 3.8 28.8 1.0
O C:HOH114 3.9 43.0 1.0
O C:HOH110 3.9 47.4 1.0
N A:ILE537 3.9 24.1 1.0
OP2 C:DA10 4.0 27.1 1.0
CA A:ILE532 4.0 23.2 1.0
N A:HIS535 4.1 26.8 1.0
CA A:LEU534 4.1 27.8 1.0
C A:GLU533 4.2 31.7 1.0
CA A:ILE537 4.2 24.2 1.0
CA A:HIS535 4.3 28.5 1.0
N A:GLY536 4.3 29.7 1.0
N A:GLU533 4.4 27.6 1.0
O A:PRO531 4.4 24.2 1.0
CG1 A:ILE532 4.5 24.8 1.0
CB A:ILE537 4.5 22.9 1.0
C A:HIS535 4.6 29.0 1.0
CA A:GLU533 4.6 30.9 1.0
N A:GLY538 4.7 24.3 1.0
O3' C:DC9 4.7 25.2 1.0
O C:HOH113 4.8 41.6 1.0
O A:GLU533 4.8 35.1 1.0
CB A:ILE532 4.9 24.6 1.0
CA A:GLY538 4.9 24.4 1.0

Reference:

H.Ouzon-Shubeita, Y.-L.Lin, S.Lee. Structure of MBD4 Bound to O6MEG:T Mispair Dna To Be Published.
Page generated: Mon Dec 14 19:17:32 2020

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