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Atomistry » Magnesium » PDB 5a28-5aby » 5a9f | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5a28-5aby » 5a9f » |
Magnesium in PDB 5a9f: Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with AdpEnzymatic activity of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp
All present enzymatic activity of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp:
2.7.7.7; Protein crystallography data
The structure of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp, PDB code: 5a9f
was solved by
J.A.Newman,
C.D.O.Cooper,
H.Aitkenhead,
D.M.Pinkas,
K.Kupinska,
N.Burgess-Brown,
F.Von Delft,
C.H.Arrowsmith,
A.Edwards,
C.Bountra,
O.Gileadi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5a9f:
The structure of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp
(pdb code 5a9f). 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 Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp, PDB code: 5a9f: Magnesium binding site 1 out of 1 in 5a9fGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp
![]() Mono view ![]() Stereo pair view
Reference:
J.A.Newman,
C.D.O.Cooper,
H.Aitkenhead,
O.Gileadi.
Structure of the Helicase Domain of Dna Polymerase Theta Reveals A Possible Role in the Microhomology-Mediated End- Joining Pathway. Structure V. 23 2319 2015.
Page generated: Sun Sep 29 00:21:37 2024
ISSN: ISSN 0969-2126 PubMed: 26636256 DOI: 10.1016/J.STR.2015.10.014 |
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