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Atomistry » Magnesium » PDB 4nya-4o5k » 4o5e » |
Magnesium in PDB 4o5e: Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable TtpEnzymatic activity of Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp
All present enzymatic activity of Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp:
2.7.7.7; Protein crystallography data
The structure of Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 4o5e
was solved by
M-.C.Koag,
S.Lee,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4o5e:
The structure of Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp
(pdb code 4o5e). 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 Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 4o5e: Magnesium binding site 1 out of 1 in 4o5eGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp
![]() Mono view ![]() Stereo pair view
Reference:
M.C.Koag,
Y.Kou,
H.Ouzon-Shubeita,
S.Lee.
Transition-State Destabilization Reveals How Human Dna Polymerase Beta Proceeds Across the Chemically Unstable Lesion N7-Methylguanine. Nucleic Acids Res. V. 42 8755 2014.
Page generated: Tue Aug 20 00:22:05 2024
ISSN: ISSN 0305-1048 PubMed: 24966350 DOI: 10.1093/NAR/GKU554 |
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