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Atomistry » Magnesium » PDB 6iux-6j7n » 6j51 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6iux-6j7n » 6j51 » |
Magnesium in PDB 6j51: Rna Polymerase II Elongation Complex Bound with SPT4/5 and Foreign Dna, Stalled at Shl(-1) of the Nucleosome, Weak ELF1 (+1 Position)Enzymatic activity of Rna Polymerase II Elongation Complex Bound with SPT4/5 and Foreign Dna, Stalled at Shl(-1) of the Nucleosome, Weak ELF1 (+1 Position)
All present enzymatic activity of Rna Polymerase II Elongation Complex Bound with SPT4/5 and Foreign Dna, Stalled at Shl(-1) of the Nucleosome, Weak ELF1 (+1 Position):
2.7.7.6; Other elements in 6j51:
The structure of Rna Polymerase II Elongation Complex Bound with SPT4/5 and Foreign Dna, Stalled at Shl(-1) of the Nucleosome, Weak ELF1 (+1 Position) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Rna Polymerase II Elongation Complex Bound with SPT4/5 and Foreign Dna, Stalled at Shl(-1) of the Nucleosome, Weak ELF1 (+1 Position)
(pdb code 6j51). 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 Rna Polymerase II Elongation Complex Bound with SPT4/5 and Foreign Dna, Stalled at Shl(-1) of the Nucleosome, Weak ELF1 (+1 Position), PDB code: 6j51: Magnesium binding site 1 out of 1 in 6j51Go back to Magnesium Binding Sites List in 6j51
Magnesium binding site 1 out
of 1 in the Rna Polymerase II Elongation Complex Bound with SPT4/5 and Foreign Dna, Stalled at Shl(-1) of the Nucleosome, Weak ELF1 (+1 Position)
Mono view Stereo pair view
Reference:
H.Ehara,
T.Kujirai,
Y.Fujino,
M.Shirouzu,
H.Kurumizaka,
S.I.Sekine.
Structural Insight Into Nucleosome Transcription By Rna Polymerase II with Elongation Factors. Science V. 363 744 2019.
Page generated: Tue Oct 1 04:35:36 2024
ISSN: ESSN 1095-9203 PubMed: 30733384 DOI: 10.1126/SCIENCE.AAV8912 |
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