Bromine 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:

Magnesium

(Mg)

5 atoms

The binding sites of Bromine 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 Bromine atom.
In total 3 binding sites of Bromine 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 Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 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 Bromine with other atoms in the Br 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:Br403 b:201.5 occ:1.00 BR A:9UE403 0.0 201.5 1.0 C28 A:9UE403 1.9 161.3 1.0 N3 A:9UE403 2.8 154.3 1.0 C21 A:9UE403 2.9 139.8 1.0 CD2 D:HIS74 3.2 70.0 1.0 CG D:HIS74 3.3 70.0 1.0 C20 A:9UE403 3.5 130.4 1.0 CB D:HIS74 3.5 70.0 1.0 OD2 D:ASP180 3.5 68.3 1.0 C27 A:9UE403 4.0 141.4 1.0 CG D:ASP180 4.0 68.3 1.0 NE2 D:HIS74 4.0 70.0 1.0 C22 A:9UE403 4.1 130.0 1.0 O3 A:9UE403 4.2 125.7 1.0 ND1 D:HIS74 4.2 70.0 1.0 OD1 D:ASP180 4.4 68.3 1.0 C9 A:9UE403 4.5 118.3 1.0 CE1 D:HIS74 4.6 70.0 1.0 C18 A:9UE403 4.7 108.6 1.0 C8 A:9UE403 4.8 121.7 1.0 CB D:ASP180 4.8 68.3 1.0 CA D:HIS74 5.0 70.0 1.0

Bromine binding site 2 out of 3 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 Bromine with other atoms in the Br 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 C:Br403 b:163.6 occ:1.00 BR C:9UE403 0.0 163.6 1.0 C28 C:9UE403 1.9 129.6 1.0 N3 C:9UE403 2.8 132.2 1.0 C21 C:9UE403 2.9 111.5 1.0 CD2 E:HIS74 3.1 68.2 1.0 CG E:HIS74 3.3 68.2 1.0 OD2 E:ASP180 3.4 64.6 1.0 C20 C:9UE403 3.5 101.6 1.0 CB E:HIS74 3.5 68.2 1.0 NE2 E:HIS74 3.9 68.2 1.0 CG E:ASP180 3.9 64.6 1.0 C27 C:9UE403 4.0 126.0 1.0 C22 C:9UE403 4.1 114.4 1.0 ND1 E:HIS74 4.1 68.2 1.0 O3 C:9UE403 4.2 102.0 1.0 OD1 E:ASP180 4.3 64.6 1.0 CE1 E:HIS74 4.4 68.2 1.0 C9 C:9UE403 4.5 100.8 1.0 C18 C:9UE403 4.7 105.1 1.0 CB E:ASP180 4.7 64.6 1.0 C8 C:9UE403 4.8 99.7 1.0

Bromine binding site 3 out of 3 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 Bromine with other atoms in the Br 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 E:Br403 b:182.9 occ:1.00 BR E:9UE403 0.0 182.9 1.0 C28 E:9UE403 1.9 136.6 1.0 N3 E:9UE403 2.8 133.8 1.0 C21 E:9UE403 2.9 116.6 1.0 CD2 A:HIS74 3.1 71.0 1.0 CG A:HIS74 3.3 71.0 1.0 C20 E:9UE403 3.5 105.6 1.0 CB A:HIS74 3.5 71.0 1.0 OD2 A:ASP180 3.5 67.7 1.0 NE2 A:HIS74 4.0 71.0 1.0 C27 E:9UE403 4.0 127.7 1.0 CG A:ASP180 4.0 67.7 1.0 C22 E:9UE403 4.1 112.1 1.0 O3 E:9UE403 4.2 118.0 1.0 ND1 A:HIS74 4.2 71.0 1.0 OD1 A:ASP180 4.4 67.7 1.0 CE1 A:HIS74 4.5 71.0 1.0 C9 E:9UE403 4.5 107.7 1.0 C18 E:9UE403 4.7 108.9 1.0 C8 E:9UE403 4.8 104.4 1.0 CB A:ASP180 4.8 67.7 1.0 CA A:HIS74 5.0 71.0 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