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Magnesium in PDB 6plc: Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable GtpEnzymatic activity of Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable Gtp
All present enzymatic activity of Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable Gtp:
2.7.7.7; Protein crystallography data
The structure of Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable Gtp, PDB code: 6plc
was solved by
M.C.Koag,
S.Lee,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable Gtp
(pdb code 6plc). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable Gtp, PDB code: 6plc: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 6plcGo back to Magnesium Binding Sites List in 6plc
Magnesium binding site 1 out
of 2 in the Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable Gtp
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 6plcGo back to Magnesium Binding Sites List in 6plc
Magnesium binding site 2 out
of 2 in the Structure of Human Dna Polymerase Eta Complexed with 8OA in the Template Base Paired with Incoming Non-Hydrolyzable Gtp
Mono view Stereo pair view
Reference:
M.C.Koag,
H.Jung,
S.Lee.
Mutagenesis Mechanism of the Major Oxidative Adenine Lesion 7,8-Dihydro-8-Oxoadenine. Nucleic Acids Res. 2020.
Page generated: Mon Dec 14 23:49:19 2020
ISSN: ESSN 1362-4962 PubMed: 32282906 DOI: 10.1093/NAR/GKAA193 |
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