Magnesium in PDB 9cfu: Cryo-Em Structure of Myosin-1C Bound to F-Actin in the Adp-A State

The binding sites of Magnesium atom in the Cryo-Em Structure of Myosin-1C Bound to F-Actin in the Adp-A State (pdb code 9cfu). 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 Myosin-1C Bound to F-Actin in the Adp-A State, PDB code: 9cfu:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Cryo-Em Structure of Myosin-1C Bound to F-Actin in the Adp-A 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 Myosin-1C Bound to F-Actin in the Adp-A State within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:80.0 occ:1.00 O3B B:ADP401 1.9 83.8 1.0 PB B:ADP401 3.3 93.8 1.0 O1B B:ADP401 3.8 94.7 1.0 OE1 B:GLN137 4.0 86.1 1.0 OD2 B:ASP11 4.1 95.5 1.0 O3A B:ADP401 4.1 87.0 1.0 O1A B:ADP401 4.1 79.6 1.0 CD B:GLN137 4.2 87.8 1.0 O2B B:ADP401 4.3 90.2 1.0 CA B:GLY13 4.3 91.4 1.0 NZ B:LYS18 4.4 81.6 1.0 NE2 B:GLN137 4.4 90.5 1.0 CA B:GLY156 4.4 80.6 1.0 OD1 B:ASP11 4.4 99.5 1.0 OD2 B:ASP154 4.5 101.8 1.0 PA B:ADP401 4.6 79.6 1.0 CG B:ASP11 4.6 94.9 1.0

Magnesium binding site 2 out of 4 in the Cryo-Em Structure of Myosin-1C Bound to F-Actin in the Adp-A 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 Myosin-1C Bound to F-Actin in the Adp-A State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg401 b:53.6 occ:1.00 OE2 C:GLU207 1.9 90.0 1.0 OE1 C:GLU207 2.0 91.5 1.0 OH C:TYR69 2.0 85.6 1.0 CD C:GLU207 2.3 89.2 1.0 CZ C:TYR69 3.0 75.4 1.0 CE2 C:TYR69 3.3 71.4 1.0 CG C:GLU207 3.8 83.6 1.0 NE C:ARG210 4.0 81.6 1.0 CD C:ARG210 4.1 76.4 1.0 CE1 C:TYR69 4.3 72.8 1.0 NE2 C:GLN59 4.3 81.0 1.0 CG2 C:ILE34 4.5 75.7 1.0 CD2 C:TYR69 4.7 76.2 1.0 CB C:GLU207 4.7 75.5 1.0 CA C:GLU207 4.7 68.0 1.0

Magnesium binding site 3 out of 4 in the Cryo-Em Structure of Myosin-1C Bound to F-Actin in the Adp-A 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 Myosin-1C Bound to F-Actin in the Adp-A State within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg401 b:62.2 occ:1.00 O1B D:ADP402 1.9 92.6 1.0 PB D:ADP402 3.1 104.3 1.0 O2B D:ADP402 3.3 85.5 1.0 O3A D:ADP402 3.8 96.2 1.0 CA D:GLY156 4.2 83.1 1.0 O1A D:ADP402 4.2 75.3 1.0 OD2 D:ASP154 4.2 98.4 1.0 CA D:GLY13 4.2 87.5 1.0 NZ D:LYS18 4.2 86.6 1.0 O3B D:ADP402 4.3 93.2 1.0 OE1 D:GLN137 4.4 93.4 1.0 NE2 D:GLN137 4.4 93.8 1.0 CD D:GLN137 4.5 92.9 1.0 PA D:ADP402 4.5 85.1 1.0 OD1 D:ASP11 4.6 101.6 1.0 OD2 D:ASP11 4.6 95.9 1.0 N D:GLY156 4.9 82.8 1.0 CG D:ASP11 5.0 96.1 1.0

Magnesium binding site 4 out of 4 in the Cryo-Em Structure of Myosin-1C Bound to F-Actin in the Adp-A 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 Myosin-1C Bound to F-Actin in the Adp-A State within 5.0Å range: probe atom residue distance (Å) B Occ P:Mg802 b:68.6 occ:1.00 O3B P:ADP801 1.9 59.6 1.0 OG1 P:THR112 2.1 108.6 1.0 OG P:SER161 2.4 104.5 1.0 CB P:THR112 3.2 110.4 1.0 PB P:ADP801 3.3 65.8 1.0 CB P:SER161 3.5 98.1 1.0 O2B P:ADP801 3.8 64.8 1.0 O3A P:ADP801 4.0 67.0 1.0 OD2 P:ASP386 4.0 115.8 1.0 CG2 P:THR112 4.1 107.7 1.0 N P:THR112 4.2 110.8 1.0 O1B P:ADP801 4.3 64.0 1.0 CA P:THR112 4.3 104.5 1.0 OD1 P:ASP386 4.5 119.2 1.0 OE2 P:GLU147 4.5 117.3 1.0 PA P:ADP801 4.7 65.6 1.0 O1A P:ADP801 4.7 65.0 1.0 CG P:ASP386 4.7 114.7 1.0 OD1 P:ASN151 4.7 101.7 1.0 CA P:SER161 4.7 101.4 1.0 NZ P:LYS111 4.7 101.5 1.0 N P:SER161 4.8 101.3 1.0 O2A P:ADP801 4.8 64.0 1.0 CE P:LYS111 4.8 105.2 1.0 ND2 P:ASN151 4.8 101.2 1.0 O P:ASN159 5.0 101.7 1.0

S.S.Chavali, C.V.Sindelar, M.E.Ostap. High Resolution Structures of Myosin-Ic Reveal A Unique Actin-Binding Orientation, Adp Release Pathway, and Power Stroke Trajectory To Be Published.