Magnesium in PDB 7aln: Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State

The structure of Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State also contains other interesting chemical elements:

Bromine

(Br)

3 atoms

The binding sites of Magnesium atom in the Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State (pdb code 7aln). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State, PDB code: 7aln:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor 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 the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:90.9 occ:1.00 O2B A:ADP401 2.0 90.9 1.0 O3B A:ADP401 2.1 90.9 1.0 PB A:ADP401 2.4 90.9 1.0 O3A A:ADP401 3.0 90.9 1.0 OE1 A:GLN138 3.6 67.1 1.0 O1B A:ADP401 3.7 90.9 1.0 NZ A:LYS19 3.9 62.5 1.0 OD2 A:ASP12 4.0 68.4 1.0 CD A:GLN138 4.2 67.1 1.0 PA A:ADP401 4.2 90.9 1.0 NE2 A:GLN138 4.4 67.1 1.0 OD1 A:ASP12 4.4 68.4 1.0 OD2 A:ASP155 4.5 67.9 1.0 O1A A:ADP401 4.5 90.9 1.0 CG2 A:VAL340 4.5 62.5 1.0 O2A A:ADP401 4.5 90.9 1.0 OD1 A:ASP155 4.5 67.9 1.0 CA A:GLY14 4.6 67.4 1.0 CG A:ASP12 4.6 68.4 1.0 CA A:GLY157 4.7 63.9 1.0 CG A:ASP155 5.0 67.9 1.0

Magnesium binding site 2 out of 5 in the Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor 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 the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:132.5 occ:1.00 O2B B:ADP401 1.8 132.7 1.0 O3B B:ADP401 2.2 132.7 1.0 PB B:ADP401 2.4 132.7 1.0 OE1 B:GLN138 2.9 66.8 1.0 O3A B:ADP401 3.4 132.7 1.0 O1B B:ADP401 3.6 132.7 1.0 CD B:GLN138 3.6 66.8 1.0 OD2 B:ASP155 3.7 66.3 1.0 NE2 B:GLN138 4.0 66.8 1.0 OD1 B:ASP155 4.0 66.3 1.0 CG B:ASP155 4.3 66.3 1.0 CG2 B:VAL340 4.4 63.1 1.0 CA B:GLY157 4.5 60.4 1.0 OD2 B:ASP12 4.5 68.1 1.0 OD1 B:ASP12 4.7 68.1 1.0 NZ B:LYS19 4.7 61.9 1.0 PA B:ADP401 4.7 132.7 1.0 CG B:GLN138 4.8 66.8 1.0 N B:GLY157 4.9 60.4 1.0 CA B:GLY14 5.0 66.3 1.0 O1A B:ADP401 5.0 132.7 1.0 CB B:GLN138 5.0 66.8 1.0

Magnesium binding site 3 out of 5 in the Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor 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 the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg402 b:84.5 occ:1.00 O2B C:ADP401 2.1 84.5 1.0 O3B C:ADP401 2.1 84.5 1.0 PB C:ADP401 2.3 84.5 1.0 O3A C:ADP401 2.7 84.5 1.0 O2A C:ADP401 3.8 84.5 1.0 O1B C:ADP401 3.8 84.5 1.0 PA C:ADP401 3.8 84.5 1.0 NZ C:LYS19 3.9 62.0 1.0 OE1 C:GLN138 3.9 67.8 1.0 OD2 C:ASP12 4.2 68.0 1.0 OD1 C:ASP155 4.4 66.9 1.0 CA C:GLY157 4.4 61.0 1.0 O1A C:ADP401 4.4 84.5 1.0 OD2 C:ASP155 4.5 66.9 1.0 CD C:GLN138 4.5 67.8 1.0 CG2 C:VAL340 4.6 62.6 1.0 NE2 C:GLN138 4.8 67.8 1.0 OD1 C:ASP12 4.8 68.0 1.0 CA C:GLY302 4.8 58.5 1.0 CA C:GLY14 4.9 66.7 1.0 CG C:ASP155 4.9 66.9 1.0 O5' C:ADP401 5.0 84.5 1.0 CG C:ASP12 5.0 68.0 1.0

Magnesium binding site 4 out of 5 in the Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor 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 the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg402 b:125.3 occ:1.00 O2B D:ADP401 1.8 127.2 1.0 O3B D:ADP401 2.1 127.2 1.0 PB D:ADP401 2.4 127.2 1.0 OE1 D:GLN138 3.2 68.6 1.0 O3A D:ADP401 3.3 127.2 1.0 O1B D:ADP401 3.6 127.2 1.0 CD D:GLN138 3.8 68.6 1.0 NE2 D:GLN138 4.1 68.6 1.0 OD2 D:ASP155 4.1 68.5 1.0 OD2 D:ASP12 4.2 71.3 1.0 OD1 D:ASP155 4.3 68.5 1.0 NZ D:LYS19 4.3 65.5 1.0 CG2 D:VAL340 4.4 65.1 1.0 OD1 D:ASP12 4.5 71.3 1.0 PA D:ADP401 4.5 127.2 1.0 CA D:GLY157 4.6 64.0 1.0 CG D:ASP155 4.6 68.5 1.0 O1A D:ADP401 4.7 127.2 1.0 CA D:GLY14 4.7 67.9 1.0 CG D:ASP12 4.8 71.3 1.0 CG D:GLN138 4.9 68.6 1.0

Magnesium binding site 5 out of 5 in the Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Cryo-Em Structure of the Divergent Actomyosin Complex From Plasmodium Falciparum Myosin A in the Rigor State within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg402 b:71.0 occ:1.00 O3B E:ADP401 2.0 70.9 1.0 O2B E:ADP401 2.2 70.9 1.0 PB E:ADP401 2.3 70.9 1.0 O3A E:ADP401 2.7 70.9 1.0 NZ E:LYS19 3.7 61.1 1.0 O1B E:ADP401 3.8 70.9 1.0 PA E:ADP401 3.8 70.9 1.0 O2A E:ADP401 4.1 70.9 1.0 OD2 E:ASP12 4.1 67.2 1.0 OE1 E:GLN138 4.1 67.0 1.0 O1A E:ADP401 4.2 70.9 1.0 OD1 E:ASP155 4.5 66.8 1.0 CG2 E:VAL340 4.5 63.5 1.0 CA E:GLY157 4.5 60.6 1.0 OD2 E:ASP155 4.6 66.8 1.0 CD E:GLN138 4.7 67.0 1.0 CA E:GLY302 4.8 58.5 1.0 OD1 E:ASP12 4.8 67.2 1.0 CE E:LYS19 4.8 61.1 1.0 CG E:ASP12 4.9 67.2 1.0 NE2 E:GLN138 4.9 67.0 1.0 CA E:GLY14 4.9 66.0 1.0

J.Robert-Paganin, X.P.Xu, M.F.Swift, D.Auguin, J.P.Robblee, H.Lu, P.M.Fagnant, E.B.Krementsova, K.M.Trybus, A.Houdusse, N.Volkmann, D.Hanein. The Actomyosin Interface Contains An Evolutionary Conserved Core and An Ancillary Interface Involved in Specificity. Nat Commun V. 12 1892 2021.
ISSN: ESSN 2041-1723
PubMed: 33767187
DOI: 10.1038/S41467-021-22093-4