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Magnesium in PDB 7dsh: Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Amppcp (E1-Atp State)

Enzymatic activity of Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Amppcp (E1-Atp State)

All present enzymatic activity of Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Amppcp (E1-Atp 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 90PS with Amppcp (E1-Atp State) (pdb code 7dsh). 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 90PS with Amppcp (E1-Atp State), PDB code: 7dsh:

Magnesium binding site 1 out of 1 in 7dsh

Go back to Magnesium Binding Sites List in 7dsh
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Amppcp (E1-Atp 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 90PS with Amppcp (E1-Atp State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1602

b:48.8
occ:1.00
O3G A:ACP1601 2.3 80.0 1.0
OD2 A:ASP1134 3.4 55.7 1.0
O A:ASP1130 3.5 43.4 1.0
O A:LYS668 3.5 43.9 1.0
OD1 A:ASP1130 3.6 43.4 1.0
N A:GLY670 3.7 41.3 1.0
PG A:ACP1601 3.7 80.0 1.0
OG1 A:THR669 4.0 48.1 1.0
CA A:GLY670 4.0 41.3 1.0
O1G A:ACP1601 4.1 80.0 1.0
CG A:ASP1134 4.4 55.7 1.0
C3B A:ACP1601 4.4 80.0 1.0
C A:THR669 4.5 48.1 1.0
OD1 A:ASN1133 4.5 59.2 1.0
C A:LYS668 4.5 43.9 1.0
C A:ASP1130 4.6 43.4 1.0
OD2 A:ASP667 4.7 41.5 1.0
CG A:ASP1130 4.7 43.4 1.0
OD1 A:ASP1134 4.8 55.7 1.0
CG A:ASP667 4.9 41.5 1.0
O2G A:ACP1601 4.9 80.0 1.0
OD1 A:ASP667 4.9 41.5 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 16:02:28 2024

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