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Magnesium in PDB 6djo: Cryo-Em Structure of Adp-Actin Filaments

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Adp-Actin Filaments (pdb code 6djo). 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 Adp-Actin Filaments, PDB code: 6djo:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 6djo

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Magnesium binding site 1 out of 4 in the Cryo-Em Structure of Adp-Actin Filaments


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 Adp-Actin Filaments within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg801

b:57.6
occ:1.00
O1B A:ADP802 2.1 59.9 1.0
PB A:ADP802 3.0 59.9 1.0
O3B A:ADP802 3.1 59.9 1.0
OE1 A:GLN137 3.3 71.3 1.0
CD A:GLN137 3.8 71.3 1.0
NE2 A:GLN137 3.9 71.3 1.0
O2B A:ADP802 4.0 59.9 1.0
O1A A:ADP802 4.0 59.9 1.0
O3A A:ADP802 4.2 59.9 1.0
CG2 A:VAL339 4.3 63.2 1.0
OD2 A:ASP11 4.5 70.0 1.0
CA A:GLY13 4.6 66.5 1.0
OD1 A:ASP11 4.7 70.0 1.0
PA A:ADP802 4.7 59.9 1.0
CB A:VAL339 4.7 63.2 1.0
NZ A:LYS18 4.9 61.4 1.0
OD1 A:ASP154 4.9 59.4 1.0
CG A:GLN137 4.9 71.3 1.0
CG1 A:VAL339 4.9 63.2 1.0
CA A:GLY156 4.9 59.1 1.0

Magnesium binding site 2 out of 4 in 6djo

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Magnesium binding site 2 out of 4 in the Cryo-Em Structure of Adp-Actin Filaments


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 Adp-Actin Filaments within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg801

b:52.4
occ:1.00
O1B B:ADP802 2.1 59.2 1.0
OE1 B:GLN137 3.1 68.1 1.0
PB B:ADP802 3.4 59.2 1.0
O3B B:ADP802 3.7 59.2 1.0
CD B:GLN137 3.8 68.1 1.0
OD1 B:ASP154 4.1 60.0 1.0
NE2 B:GLN137 4.2 68.1 1.0
CA B:GLY156 4.2 57.5 1.0
O1A B:ADP802 4.2 59.2 1.0
O3A B:ADP802 4.3 59.2 1.0
CG2 B:VAL339 4.4 61.9 1.0
O2B B:ADP802 4.5 59.2 1.0
OD2 B:ASP154 4.7 60.0 1.0
CG B:ASP154 4.8 60.0 1.0
CG B:GLN137 4.9 68.1 1.0
PA B:ADP802 4.9 59.2 1.0
N B:GLY156 5.0 57.5 1.0
CA B:GLY301 5.0 58.1 1.0

Magnesium binding site 3 out of 4 in 6djo

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Magnesium binding site 3 out of 4 in the Cryo-Em Structure of Adp-Actin Filaments


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 Adp-Actin Filaments within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg801

b:54.0
occ:1.00
O1B C:ADP802 2.1 58.5 1.0
O2B C:ADP802 2.6 58.5 1.0
PB C:ADP802 2.8 58.5 1.0
OE1 C:GLN137 3.7 65.5 1.0
O3A C:ADP802 3.7 58.5 1.0
O1A C:ADP802 3.9 58.5 1.0
O3B C:ADP802 4.1 58.5 1.0
CD C:GLN137 4.2 65.5 1.0
NE2 C:GLN137 4.3 65.5 1.0
PA C:ADP802 4.4 58.5 1.0
CG2 C:VAL339 4.4 57.6 1.0
NZ C:LYS18 4.6 58.3 1.0
OD2 C:ASP11 4.6 65.5 1.0
CA C:GLY156 4.7 55.8 1.0
CA C:GLY13 4.8 62.8 1.0
CB C:VAL339 4.8 57.6 1.0
OD1 C:ASP154 4.9 57.5 1.0
OD1 C:ASP11 5.0 65.5 1.0

Magnesium binding site 4 out of 4 in 6djo

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Magnesium binding site 4 out of 4 in the Cryo-Em Structure of Adp-Actin Filaments


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 Adp-Actin Filaments within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg801

b:62.7
occ:1.00
O1B D:ADP802 2.1 60.6 1.0
O3B D:ADP802 2.1 60.6 1.0
PB D:ADP802 2.5 60.6 1.0
O1A D:ADP802 3.3 60.6 1.0
O3A D:ADP802 3.6 60.6 1.0
O2B D:ADP802 3.7 60.6 1.0
PA D:ADP802 3.9 60.6 1.0
NZ D:LYS18 3.9 59.1 1.0
OE1 D:GLN137 4.3 63.5 1.0
O2A D:ADP802 4.5 60.6 1.0
CA D:GLY13 4.5 63.1 1.0
OD2 D:ASP11 4.5 66.6 1.0
NE2 D:GLN137 4.7 63.5 1.0
CG2 D:VAL339 4.7 59.1 1.0
CD D:GLN137 4.7 63.5 1.0
CA D:GLY156 4.9 57.7 1.0
CE D:LYS18 4.9 59.1 1.0
OD1 D:ASP11 5.0 66.6 1.0

Reference:

S.Z.Chou, T.D.Pollard. Mechanism of Actin Polymerization Revealed By Cryo-Em Structures of Actin Filaments with Three Different Bound Nucleotides. Proc.Natl.Acad.Sci.Usa V. 116 4265 2019.
ISSN: ESSN 1091-6490
PubMed: 30760599
DOI: 10.1073/PNAS.1807028115
Page generated: Mon Sep 30 23:10:13 2024

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