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Atomistry » Magnesium » PDB 5v6s-5vp0 » 5vi8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5v6s-5vp0 » 5vi8 » |
Magnesium in PDB 5vi8: Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter FragmentEnzymatic activity of Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter Fragment
All present enzymatic activity of Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter Fragment:
2.7.7.6; Protein crystallography data
The structure of Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter Fragment, PDB code: 5vi8
was solved by
E.A.Hubin,
E.A.Campbell,
S.A.Darst,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5vi8:
The structure of Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter Fragment also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter Fragment
(pdb code 5vi8). 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 Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter Fragment, PDB code: 5vi8: Magnesium binding site 1 out of 1 in 5vi8Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Structure of A Mycobacterium Smegmatis Transcription Initiation Complex with An Upstream-Fork Promoter Fragment
![]() Mono view ![]() Stereo pair view
Reference:
E.A.Hubin,
M.Lilic,
S.A.Darst,
E.A.Campbell.
Structural Insights Into the Mycobacteria Transcription Initiation Complex From Analysis of X-Ray Crystal Structures. Nat Commun V. 8 16072 2017.
Page generated: Mon Sep 30 06:10:32 2024
ISSN: ESSN 2041-1723 PubMed: 28703128 DOI: 10.1038/NCOMMS16072 |
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