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Atomistry » Sodium » PDB 8emd-8f6b » 8eng | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 8emd-8f6b » 8eng » |
Sodium in PDB 8eng: Human Pu.1 Ets-Domain (165-270) Bound to D(Aataagcggaagtggg) with Hemi-Methylated Cpg (Forward Strand)Protein crystallography data
The structure of Human Pu.1 Ets-Domain (165-270) Bound to D(Aataagcggaagtggg) with Hemi-Methylated Cpg (Forward Strand), PDB code: 8eng
was solved by
J.R.Terrell,
G.M.K.Poon,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Human Pu.1 Ets-Domain (165-270) Bound to D(Aataagcggaagtggg) with Hemi-Methylated Cpg (Forward Strand)
(pdb code 8eng). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Human Pu.1 Ets-Domain (165-270) Bound to D(Aataagcggaagtggg) with Hemi-Methylated Cpg (Forward Strand), PDB code: 8eng: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 8engGo back to![]() ![]()
Sodium binding site 1 out
of 2 in the Human Pu.1 Ets-Domain (165-270) Bound to D(Aataagcggaagtggg) with Hemi-Methylated Cpg (Forward Strand)
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 8engGo back to![]() ![]()
Sodium binding site 2 out
of 2 in the Human Pu.1 Ets-Domain (165-270) Bound to D(Aataagcggaagtggg) with Hemi-Methylated Cpg (Forward Strand)
![]() Mono view ![]() Stereo pair view
Reference:
J.R.Terrell,
S.J.Taylor,
A.L.Schneider,
Y.Lu,
T.N.Vernon,
S.Xhani,
R.H.Gumpper,
M.Luo,
W.D.Wilson,
U.Steidl,
G.M.K.Poon.
Dna Selection By the Master Transcription Factor Pu.1. Cell Rep V. 42 12671 2023.
Page generated: Mon Aug 18 14:02:02 2025
ISSN: ESSN 2211-1247 PubMed: 37352101 DOI: 10.1016/J.CELREP.2023.112671 |
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