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Magnesium in PDB 8e8j: Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+

Enzymatic activity of Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+

All present enzymatic activity of Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+:
2.7.7.7;

Protein crystallography data

The structure of Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+, PDB code: 8e8j was solved by C.Chang, Y.Gao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.01 / 2.40
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.019, 98.019, 81.849, 90, 90, 120
R / Rfree (%) 19.2 / 21.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+ (pdb code 8e8j). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+, PDB code: 8e8j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 8e8j

Go back to Magnesium Binding Sites List in 8e8j
Magnesium binding site 1 out of 2 in the Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:21.9
occ:1.00
OD2 A:ASP115 2.0 27.5 1.0
OD1 A:ASP13 2.0 20.8 1.0
O2G A:XG4503 2.0 17.7 1.0
O A:MET14 2.0 18.1 1.0
O1B A:XG4503 2.2 20.1 1.0
O1A A:XG4503 2.5 39.6 1.0
CG A:ASP13 3.0 20.6 1.0
CG A:ASP115 3.0 22.9 1.0
PB A:XG4503 3.1 20.8 1.0
PA A:XG4503 3.2 23.5 1.0
C A:MET14 3.2 24.2 1.0
OD2 A:ASP13 3.3 26.5 1.0
PG A:XG4503 3.3 24.7 1.0
N3A A:XG4503 3.4 25.4 1.0
O5' A:XG4503 3.4 36.4 1.0
O3B A:XG4503 3.5 19.7 1.0
OD1 A:ASP115 3.5 25.0 1.0
MG A:MG502 3.7 20.9 1.0
N A:MET14 3.7 28.5 1.0
O3G A:XG4503 3.9 25.1 1.0
CA A:MET14 4.0 24.9 1.0
NZ A:LYS231 4.1 20.8 1.0
C A:ASP13 4.2 22.3 1.0
CB A:ASP115 4.3 13.1 1.0
N A:ASP15 4.3 18.8 1.0
CB A:ASP13 4.3 21.6 1.0
O A:HOH603 4.4 22.1 1.0
O1G A:XG4503 4.4 25.7 1.0
N A:CYS16 4.4 22.1 1.0
CB A:MET14 4.5 24.9 1.0
O2B A:XG4503 4.5 24.7 1.0
CA A:ASP15 4.5 23.7 1.0
N A:PHE17 4.6 23.9 1.0
CB A:PHE17 4.6 18.5 1.0
O2A A:XG4503 4.6 22.6 1.0
C A:ASP15 4.7 24.7 1.0
CA A:ASP13 4.7 20.6 1.0
O A:ASP13 4.7 20.3 1.0
C5' A:XG4503 4.9 29.2 1.0
O A:ASP115 4.9 29.6 1.0
CE A:LYS231 4.9 26.7 1.0

Magnesium binding site 2 out of 2 in 8e8j

Go back to Magnesium Binding Sites List in 8e8j
Magnesium binding site 2 out of 2 in the Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Dna Polymerase Eta-Dna-Rg-Ended Primer-Dgmpnpp Ternary Mismatch Complex with MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:20.9
occ:1.00
OE1 A:GLU116 2.0 39.9 1.0
O A:HOH603 2.0 22.1 1.0
O A:HOH607 2.1 22.5 1.0
OD1 A:ASP115 2.1 25.0 1.0
OD2 A:ASP13 2.2 26.5 1.0
O1A A:XG4503 2.4 39.6 1.0
CD A:GLU116 3.0 25.4 1.0
CG A:ASP115 3.1 22.9 1.0
PA A:XG4503 3.2 23.5 1.0
CG A:ASP13 3.3 20.6 1.0
O5' A:XG4503 3.4 36.4 1.0
OD2 A:ASP115 3.5 27.5 1.0
OG A:SER113 3.5 26.4 1.0
O2A A:XG4503 3.7 22.6 1.0
MG A:MG501 3.7 21.9 1.0
OD1 A:ASP13 3.8 20.8 1.0
OE2 A:GLU116 3.8 29.5 1.0
CG A:GLU116 4.0 30.2 1.0
CB A:GLU116 4.1 17.9 1.0
C5' A:XG4503 4.2 29.2 1.0
NZ A:LYS224 4.4 17.2 1.0
CB A:ASP115 4.5 13.1 1.0
CB A:ASP13 4.5 21.6 1.0
C A:ASP115 4.6 17.0 1.0
CB A:SER113 4.6 19.8 1.0
OP1 P:G9 4.7 35.1 1.0
O2' P:G9 4.7 39.4 1.0
O2G A:XG4503 4.7 17.7 1.0
O A:ASP115 4.7 29.6 1.0
N3A A:XG4503 4.7 25.4 1.0
N A:GLU116 4.8 30.9 1.0
CA A:ASP115 4.9 22.7 1.0

Reference:

C.Chang, C.Lee Luo, S.Eleraky, A.Lin, G.Zhou, Y.Gao. Primer Terminal Ribonucleotide Alters the Active Site Dynamics of Dna Polymerase Eta and Reduce Dna Synthesis Fidelity J.Biol.Chem. 02938 2023.
ISSN: ESSN 1083-351X
DOI: 10.1016/J.JBC.2023.102938
Page generated: Fri Aug 15 03:40:00 2025

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