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Atomistry » Potassium » PDB 5f6q-5g13 » 5fg0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 5f6q-5g13 » 5fg0 » |
Potassium in PDB 5fg0: Structure of the Conserved Yeast Listerin (LTN1) N-Terminal Domain, Monoclinic FormProtein crystallography data
The structure of Structure of the Conserved Yeast Listerin (LTN1) N-Terminal Domain, Monoclinic Form, PDB code: 5fg0
was solved by
S.K.Doamekpor,
C.D.Lima,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of the Conserved Yeast Listerin (LTN1) N-Terminal Domain, Monoclinic Form
(pdb code 5fg0). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of the Conserved Yeast Listerin (LTN1) N-Terminal Domain, Monoclinic Form, PDB code: 5fg0: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 5fg0Go back to Potassium Binding Sites List in 5fg0
Potassium binding site 1 out
of 2 in the Structure of the Conserved Yeast Listerin (LTN1) N-Terminal Domain, Monoclinic Form
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 5fg0Go back to Potassium Binding Sites List in 5fg0
Potassium binding site 2 out
of 2 in the Structure of the Conserved Yeast Listerin (LTN1) N-Terminal Domain, Monoclinic Form
Mono view Stereo pair view
Reference:
S.K.Doamekpor,
J.W.Lee,
N.L.Hepowit,
C.Wu,
C.Charenton,
M.Leonard,
M.H.Bengtson,
K.R.Rajashankar,
M.S.Sachs,
C.D.Lima,
C.A.Joazeiro.
Structure and Function of the Yeast Listerin (LTN1) Conserved N-Terminal Domain in Binding to Stalled 60S Ribosomal Subunits. Proc.Natl.Acad.Sci.Usa V. 113 E4151 2016.
Page generated: Mon Aug 12 13:31:28 2024
ISSN: ESSN 1091-6490 PubMed: 27385828 DOI: 10.1073/PNAS.1605951113 |
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