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Atomistry » Magnesium » PDB 4z4g-4zhq » 4z6d » |
Magnesium in PDB 4z6d: Structure of Human Dna Polymerase Beta 279NA Mutant Complexed with G in the Template Base Paired with Incoming Non-Hydrolyzable TtpEnzymatic activity of Structure of Human Dna Polymerase Beta 279NA Mutant Complexed with G in the Template Base Paired with Incoming Non-Hydrolyzable Ttp
All present enzymatic activity of Structure of Human Dna Polymerase Beta 279NA Mutant Complexed with G 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 Beta 279NA Mutant Complexed with G in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 4z6d
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 4z6d:
The structure of Structure of Human Dna Polymerase Beta 279NA Mutant Complexed with G 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 Beta 279NA Mutant Complexed with G in the Template Base Paired with Incoming Non-Hydrolyzable Ttp
(pdb code 4z6d). 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 Beta 279NA Mutant Complexed with G in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 4z6d: Magnesium binding site 1 out of 1 in 4z6dGo back to Magnesium Binding Sites List in 4z6d
Magnesium binding site 1 out
of 1 in the Structure of Human Dna Polymerase Beta 279NA Mutant Complexed with G in the Template Base Paired with Incoming Non-Hydrolyzable Ttp
Mono view Stereo pair view
Reference:
M.C.Koag,
S.Lee.
Insights Into the Effect of Minor Groove Interactions and Metal Cofactors on Mutagenic Replication By Human Dna Polymerase Beta. Biochem. J. V. 475 571 2018.
Page generated: Mon Dec 14 19:56:38 2020
ISSN: ESSN 1470-8728 PubMed: 29301983 DOI: 10.1042/BCJ20170787 |
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