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Atomistry » Magnesium » PDB 5lu4-5m5c » 5m1m | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5lu4-5m5c » 5m1m » |
Magnesium in PDB 5m1m: Crystal Structure of Matrix Protein 1 From Influenza C Virus (Strain C/Ann Arbor/1/1950)Protein crystallography data
The structure of Crystal Structure of Matrix Protein 1 From Influenza C Virus (Strain C/Ann Arbor/1/1950), PDB code: 5m1m
was solved by
J.Radzimanowski,
W.Weissenhorn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Matrix Protein 1 From Influenza C Virus (Strain C/Ann Arbor/1/1950)
(pdb code 5m1m). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Matrix Protein 1 From Influenza C Virus (Strain C/Ann Arbor/1/1950), PDB code: 5m1m: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 5m1mGo back to Magnesium Binding Sites List in 5m1m
Magnesium binding site 1 out
of 2 in the Crystal Structure of Matrix Protein 1 From Influenza C Virus (Strain C/Ann Arbor/1/1950)
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 5m1mGo back to Magnesium Binding Sites List in 5m1m
Magnesium binding site 2 out
of 2 in the Crystal Structure of Matrix Protein 1 From Influenza C Virus (Strain C/Ann Arbor/1/1950)
Mono view Stereo pair view
Reference:
D.Saletti,
J.Radzimanowski,
G.Effantin,
D.Midtvedt,
S.Mangenot,
W.Weissenhorn,
P.Bassereau,
M.Bally.
The Matrix Protein M1 From Influenza C Virus Induces Tubular Membrane Invaginations in An in Vitro Cell Membrane Model. Sci Rep V. 7 40801 2017.
Page generated: Sun Sep 29 21:08:27 2024
ISSN: ESSN 2045-2322 PubMed: 28120862 DOI: 10.1038/SREP40801 |
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