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Magnesium in PDB 8p2i: Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5
Enzymatic activity of Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5
All present enzymatic activity of Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5:
2.7.7.6;
2.7.7.6;
Other elements in 8p2i:
The structure of Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5 also contains other interesting chemical elements:
| Zinc | (Zn) | 6 atoms |
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5
(pdb code 8p2i). 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 Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5, PDB code: 8p2i:
In total only one binding site of Magnesium was determined in the Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5, PDB code: 8p2i:
Magnesium binding site 1 out of 1 in 8p2i
Go back to
Magnesium Binding Sites List in 8p2i
Magnesium binding site 1 out
of 1 in the Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Cryo-Em Structure of Pyrococcus Furiosus Apo Form Rna Polymerase Contracted Clamp Conformation with SPT4/5 within 5.0Å range:
|
Reference:
D.M.Tarau,
F.Grunberger,
M.Pilsl,
R.Reichelt,
F.B.Heiss,
S.Koenig,
H.Urlaub,
W.Hausner,
C.Engel,
D.Grohmann.
Structural Basis of Archaeal Rna Polymerase Transcription Elongation and SPT4/5 Recruitment Nucleic Acids Res. 2024.
ISSN: ESSN 1362-4962
Page generated: Fri Oct 4 15:13:24 2024
ISSN: ESSN 1362-4962
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