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Magnesium in PDB 8jfz: Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State.

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State. (pdb code 8jfz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State., PDB code: 8jfz:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 8jfz

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Magnesium binding site 1 out of 4 in the Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ 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 Na+,K+-Atpase in the E1.MG2+ State. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1111

b:28.8
occ:1.00
OD1 C:ASP811 2.1 24.9 1.0
OG C:SER782 2.1 24.6 1.0
OE2 C:GLU786 2.4 21.7 1.0
O C:HOH2101 2.5 22.3 1.0
O C:HOH2103 2.5 25.6 1.0
CG C:ASP811 3.0 24.9 1.0
CB C:SER782 3.0 24.6 1.0
OD2 C:ASP811 3.3 24.9 1.0
CD C:GLU786 3.6 21.7 1.0
O C:THR779 3.9 20.0 1.0
OE1 C:GLU786 4.1 21.7 1.0
CA C:SER782 4.2 24.6 1.0
CB C:ASP811 4.3 24.9 1.0
C C:SER782 4.3 24.6 1.0
CA C:ASP811 4.5 24.9 1.0
ND2 C:ASN783 4.5 23.1 1.0
O C:SER782 4.6 24.6 1.0
CG2 C:ILE810 4.7 23.1 1.0
N C:SER782 4.7 24.6 1.0
N C:ASN783 4.7 23.1 1.0
CG C:GLU786 4.8 21.7 1.0
N C:ASP811 4.9 24.9 1.0

Magnesium binding site 2 out of 4 in 8jfz

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Magnesium binding site 2 out of 4 in the Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1112

b:65.2
occ:1.00
O C:HOH2102 2.4 52.6 1.0
OD1 C:ASP747 3.0 50.2 1.0
OD2 C:ASP747 3.7 50.2 1.0
CG C:ASP747 3.7 50.2 1.0
O C:LYS726 3.8 66.0 1.0
CA C:LYS726 4.5 66.0 1.0
C C:LYS726 4.6 66.0 1.0
CD C:LYS726 4.6 66.0 1.0
O C:LEU725 4.6 66.3 1.0
CE C:LYS726 4.6 66.0 1.0
O C:ALA728 4.6 59.9 1.0
CG C:LYS726 4.7 66.0 1.0
O C:ALA745 4.9 63.5 1.0

Magnesium binding site 3 out of 4 in 8jfz

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Magnesium binding site 3 out of 4 in the Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1113

b:27.7
occ:1.00
OD1 A:ASP811 2.1 23.4 1.0
OG A:SER782 2.1 22.0 1.0
OE2 A:GLU786 2.4 19.4 1.0
O A:HOH2101 2.4 18.6 1.0
O A:HOH2103 2.6 21.4 1.0
CG A:ASP811 3.0 23.4 1.0
CB A:SER782 3.0 22.0 1.0
OD2 A:ASP811 3.3 23.4 1.0
CD A:GLU786 3.6 19.4 1.0
O A:THR779 3.9 19.8 1.0
OE1 A:GLU786 4.1 19.4 1.0
CA A:SER782 4.2 22.0 1.0
CB A:ASP811 4.3 23.4 1.0
C A:SER782 4.3 22.0 1.0
CA A:ASP811 4.5 23.4 1.0
ND2 A:ASN783 4.5 21.6 1.0
O A:SER782 4.6 22.0 1.0
CG2 A:ILE810 4.7 22.2 1.0
N A:SER782 4.7 22.0 1.0
N A:ASN783 4.7 21.6 1.0
CG A:GLU786 4.8 19.4 1.0
N A:ASP811 4.9 23.4 1.0

Magnesium binding site 4 out of 4 in 8jfz

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Magnesium binding site 4 out of 4 in the Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cryo-Em Structure of Na+,K+-Atpase in the E1.MG2+ State. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1114

b:53.1
occ:1.00
O A:HOH2102 2.2 47.4 1.0
OD1 A:ASP747 3.0 44.7 1.0
OD2 A:ASP747 3.7 44.7 1.0
CG A:ASP747 3.7 44.7 1.0
O A:LYS726 3.8 64.0 1.0
CA A:LYS726 4.5 64.0 1.0
C A:LYS726 4.6 64.0 1.0
CD A:LYS726 4.6 64.0 1.0
O A:LEU725 4.6 63.8 1.0
CE A:LYS726 4.6 64.0 1.0
O A:ALA728 4.6 56.8 1.0
CG A:LYS726 4.7 64.0 1.0
O A:ALA745 4.9 58.9 1.0

Reference:

R.Kanai, B.Vilsen, F.Cornelius, C.Toyoshima. Crystal Structures of Na + ,K + -Atpase Reveal the Mechanism That Converts the K + -Bound Form to Na + -Bound Form and Opens and Closes the Cytoplasmic Gate. Febs Lett. 2023.
ISSN: ISSN 0014-5793
PubMed: 37357620
DOI: 10.1002/1873-3468.14689
Page generated: Thu Dec 28 09:35:37 2023

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