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Atomistry » Magnesium » PDB 5vw9-5w4u » 5vz8 » |
Magnesium in PDB 5vz8: Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming UtpEnzymatic activity of Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp
All present enzymatic activity of Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp:
2.7.7.7; Protein crystallography data
The structure of Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp, PDB code: 5vz8
was solved by
A.F.Moon,
J.M.Pryor,
D.A.Ramsden,
T.A.Kunkel,
K.Bebenek,
L.C.Pedersen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5vz8:
The structure of Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp
(pdb code 5vz8). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp, PDB code: 5vz8: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 5vz8Go back to Magnesium Binding Sites List in 5vz8
Magnesium binding site 1 out
of 2 in the Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 5vz8Go back to Magnesium Binding Sites List in 5vz8
Magnesium binding site 2 out
of 2 in the Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Utp
Mono view Stereo pair view
Reference:
A.F.Moon,
J.M.Pryor,
D.A.Ramsden,
T.A.Kunkel,
K.Bebenek,
L.C.Pedersen.
Structural Accommodation of Ribonucleotide Incorporation By the Dna Repair Enzyme Polymerase Mu. Nucleic Acids Res. V. 45 9138 2017.
Page generated: Mon Sep 30 06:22:54 2024
ISSN: ESSN 1362-4962 PubMed: 28911097 DOI: 10.1093/NAR/GKX527 |
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