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Atomistry » Sodium » PDB 6bg0-6c0l » 6bkg | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 6bg0-6c0l » 6bkg » |
Sodium in PDB 6bkg: Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed ConformationEnzymatic activity of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation
All present enzymatic activity of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation:
6.5.1.1; Protein crystallography data
The structure of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation, PDB code: 6bkg
was solved by
A.F.Moon,
P.P.Tumbale,
M.J.Schellenberg,
R.S.Williams,
J.G.Williams,
T.A.Kunkel,
L.C.Pedersen,
B.Bebenek,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6bkg:
The structure of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation
(pdb code 6bkg). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation, PDB code: 6bkg: Sodium binding site 1 out of 1 in 6bkgGo back to![]() ![]()
Sodium binding site 1 out
of 1 in the Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation
![]() Mono view ![]() Stereo pair view
Reference:
A.M.Kaminski,
P.P.Tumbale,
M.J.Schellenberg,
R.S.Williams,
J.G.Williams,
T.A.Kunkel,
L.C.Pedersen,
K.Bebenek.
Structures of Dna-Bound Human Ligase IV Catalytic Core Reveal Insights Into Substrate Binding and Catalysis. Nat Commun V. 9 2642 2018.
Page generated: Tue Oct 8 02:11:44 2024
ISSN: ESSN 2041-1723 PubMed: 29980672 DOI: 10.1038/S41467-018-05024-8 |
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