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Atomistry » Magnesium » PDB 4y2q-4y8m » 4y52 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 4y2q-4y8m » 4y52 » |
Magnesium in PDB 4y52: Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.Enzymatic activity of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
All present enzymatic activity of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.:
2.7.7.6; Protein crystallography data
The structure of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation., PDB code: 4y52
was solved by
L.Wang,
J.Chong,
D.Wang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4y52:
The structure of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
(pdb code 4y52). 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 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation., PDB code: 4y52: Magnesium binding site 1 out of 1 in 4y52Go back to Magnesium Binding Sites List in 4y52
Magnesium binding site 1 out
of 1 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view Stereo pair view
Reference:
L.Wang,
Y.Zhou,
L.Xu,
R.Xiao,
X.Lu,
L.Chen,
J.Chong,
H.Li,
C.He,
X.D.Fu,
D.Wang.
Molecular Basis For 5-Carboxycytosine Recognition By Rna Polymerase II Elongation Complex. Nature V. 523 621 2015.
Page generated: Mon Dec 14 19:49:24 2020
ISSN: ESSN 1476-4687 PubMed: 26123024 DOI: 10.1038/NATURE14482 |
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