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Magnesium in PDB 7drx: Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Beryllium Fluoride (E2P State)

Enzymatic activity of Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Beryllium Fluoride (E2P State)

All present enzymatic activity of Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Beryllium Fluoride (E2P State):
7.6.2.1;

Other elements in 7drx:

The structure of Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Beryllium Fluoride (E2P State) also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Beryllium Fluoride (E2P State) (pdb code 7drx). 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 Beryllium Fluoride (E2P State), PDB code: 7drx:

Magnesium binding site 1 out of 1 in 7drx

Go back to Magnesium Binding Sites List in 7drx
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of DNF1 From Saccharomyces Cerevisiae in 90PS with Beryllium Fluoride (E2P 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 Beryllium Fluoride (E2P State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1601

b:18.1
occ:1.00
OD1 A:ASP667 2.1 17.5 1.0
OD2 A:ASP667 2.2 17.5 1.0
CG A:ASP667 2.5 17.5 1.0
F2 A:BEF1602 3.4 19.6 1.0
BE A:BEF1602 3.4 19.6 1.0
NZ A:LYS1110 3.6 20.4 1.0
N A:GLY990 3.6 27.2 1.0
CA A:GLY440 3.8 29.8 1.0
N A:THR669 3.8 19.8 1.0
ND2 A:ASN1133 3.9 22.6 1.0
N A:LYS668 3.9 20.2 1.0
CB A:ASP667 3.9 17.5 1.0
F1 A:BEF1602 4.1 19.6 1.0
F3 A:BEF1602 4.1 19.6 1.0
N A:GLY440 4.1 29.8 1.0
CB A:THR669 4.2 19.8 1.0
CA A:GLY990 4.3 27.2 1.0
O A:THR669 4.3 19.8 1.0
O A:ASP439 4.3 31.4 1.0
C A:ASP439 4.5 31.4 1.0
CA A:THR669 4.5 19.8 1.0
OG1 A:THR669 4.5 19.8 1.0
C A:THR989 4.5 23.0 1.0
O A:LEU988 4.6 16.8 1.0
CA A:ASP667 4.6 17.5 1.0
CA A:THR989 4.6 23.0 1.0
C A:LYS668 4.7 20.2 1.0
OD1 A:ASN1133 4.7 22.6 1.0
CG A:ASN1133 4.7 22.6 1.0
CA A:LYS668 4.7 20.2 1.0
C A:ASP667 4.7 17.5 1.0
OD2 A:ASP1134 4.7 20.1 1.0
OD1 A:ASP1134 4.7 20.1 1.0
CE A:LYS1110 4.8 20.4 1.0
C A:THR669 4.9 19.8 1.0
CB A:LYS668 4.9 20.2 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 16:01:38 2024

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