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Magnesium in PDB 7dsi: Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in Yeast Lipids with Amppcp ( Resting State )

Enzymatic activity of Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in Yeast Lipids with Amppcp ( Resting State )

All present enzymatic activity of Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in Yeast Lipids with Amppcp ( Resting State ):
7.6.2.1;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in Yeast Lipids with Amppcp ( Resting State ) (pdb code 7dsi). 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 DNF1 From Saccharomyces Cerevisiae in Yeast Lipids with Amppcp ( Resting State ), PDB code: 7dsi:

Magnesium binding site 1 out of 1 in 7dsi

Go back to Magnesium Binding Sites List in 7dsi
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in Yeast Lipids with Amppcp ( Resting State )


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 DNF1 From Saccharomyces Cerevisiae in Yeast Lipids with Amppcp ( Resting State ) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1602

b:22.9
occ:1.00
O A:THR669 2.7 26.8 1.0
OD2 A:ASP667 2.8 21.6 1.0
O3G A:ACP1601 3.1 46.2 1.0
O A:ASP1130 3.4 15.2 1.0
OD1 A:ASP1130 3.5 15.2 1.0
C A:THR669 3.8 26.8 1.0
CG A:ASP667 3.8 21.6 1.0
CG2 A:THR669 4.1 26.8 1.0
C A:ASP1130 4.2 15.2 1.0
OD1 A:ASN1133 4.2 39.8 1.0
CG A:ASP1130 4.4 15.2 1.0
OD1 A:ASP667 4.5 21.6 1.0
PG A:ACP1601 4.5 46.2 1.0
CA A:GLY1131 4.5 37.0 1.0
N A:GLY670 4.6 19.5 1.0
CA A:GLY670 4.6 19.5 1.0
OE2 A:GLU1151 4.6 84.6 1.0
CB A:ASP667 4.7 21.6 1.0
N A:GLY1131 4.7 37.0 1.0
CA A:THR669 4.7 26.8 1.0
O2G A:ACP1601 4.7 46.2 1.0
O2B A:ACP1601 4.8 46.2 1.0
N A:THR669 4.8 26.8 1.0
N A:ASP1130 5.0 15.2 1.0

Reference:

J.Xu, Y.He, X.Wu, L.Li. Conformational Changes of A Phosphatidylcholine Flippase in Lipid Membranes. Cell Rep V. 38 10518 2022.
ISSN: ESSN 2211-1247
PubMed: 35294892
DOI: 10.1016/J.CELREP.2022.110518
Page generated: Wed Oct 2 16:03:10 2024

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